Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2'-methyladenosine 5'-diphosphate + reduced dithiothreitol
adenine + 2'-deoxy-2'-methyladenosine + H2O
-
-
5% reduction to 2'-deoxy-2'-methyladenosine, adenine is the major product besides other unidentified products
?
2'-methyluridine 5'-diphosphate + reduced dithiothreitol
uracil + H2O + ?
-
-
uracil is the major product, unidentified minor product may be 2'-deoxy-2'-methyluridine
?
2,6-diaminopurineriboside diphosphate + reduced thioredoxin
2'-deoxy-2,6-diaminopurineriboside diphosphate + H2O
-
-
-
?
2-aminopurineriboside diphosphate + reduced thioredoxin
2'-deoxy-2-aminopurineriboside diphosphate + H2O
-
-
-
?
8-vinyl-ADP + reduced thioredoxin
8-vinyl-2'-deoxy-ADP + thioredoxin disulfide + H2O
-
-
-
-
?
ADP + dithiothreitol
2'-dADP + oxidized dithiothreitol + H2O
-
-
-
?
ADP + reduced dithiothreitol
2'-dADP + oxidized dithiothreitol + H2O
-
-
-
-
r
ADP + reduced thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
-
?
ADP + reduced thioredoxin
2'-deoxy-ADP + oxidized thioredoxin + H2O
-
-
-
ir
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
benzimidazoleriboside diphosphate + reduced thioredoxin
2'-deoxybenzimidazolriboside diphosphate + H2O
-
-
-
?
CDP + dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
CDP + reduced dithiothreitol
dCDP + oxidized dithiothreitol + H2O
-
-
-
-
r
CDP + reduced glutaredoxin 1
dCDP + oxidized glutaredoxin 1 + H2O
-
-
-
-
r
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
CDP + reduced thioredoxin
2'-deoxy-CDP + oxidized thioredoxin + H2O
-
-
-
ir
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
CDP + thioredoxin
dCDP + thioredoxin disulfide + H2O
CDP + thioredoxin A
2'-dCDP + thioredoxin A disulfide + H2O
CDP + thioredoxin YosR
2'-dCDP + thioredoxin YosR disulfide + H2O
CTP + reduced thioredoxin
2'-dCTP + thioredoxin disulfide + H2O
-
-
-
-
?
dCDP + DTT disulfide + H2O
CDP + DTT
GDP + reduced thioredoxin
2'-deoxy-GDP + oxidized thioredoxin + H2O
-
-
-
ir
GDP + reduced thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
-
-
-
?
GDP + thioredoxin
2'-deoxyGDP + thioredoxin disulfide + H2O
-
-
-
?
GDP + thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
purineriboside diphosphate + reduced thioredoxin
2'-deoxypurineriboside diphosphate + H2O
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
ribonucleoside diphosphate + reduced glutaredoxin
2'-deoxyribonucleoside diphosphate + oxidized glutaredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced glutaredoxin 1
2'-deoxyribonucleoside diphosphate + oxidized glutaredoxin 1 + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
tubercidin diphosphate + reduced thioredoxin
2'-deoxytubercidin diphosphate + oxidized thioredoxin + H2O
-
14% of GDP reduction rate
-
?
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
additional information
?
-
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
Herpes simplex virus
-
-
-
-
r
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
-
r
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
Tequatrovirus T4
-
-
-
-
r
CDP + dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
?
CDP + dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
?
CDP + dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
?
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
r
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
?
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
r
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
-
?
CDP + reduced dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductase
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
Herpes simplex virus
-
-
-
-
r
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
for ATP-bound enzyme CDP is the favored substrate
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
r
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
CDP is the favored substrate. However, the kcat/Km values for ADP, GDP, and UDP are within 100-fold of the value for CDP
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
r
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
Tequatrovirus T4
-
-
-
-
r
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
coupled assay method with NADPH, transient spectrometric measurement of Y356 radical intermediate, Y356 radical initiation is prompted by excitation of a proximal anthraquinone or benzophenone chromophore on a 20-mer peptide Y-R2C19, bound to subunit alpha2, both the Anq and BPA-containing peptides are competent in deoxycytidine diphosphate formation and turnover occurs via Y731 to Y730 to C439 pathway-dependent radical transport in R1, overview. Peptide Y-R2C19 is identical to the C-terminal peptide tail of the R2 subunit and is a known competitive inhibitor of binding of the native R2 protein to R1
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
dCDP + thioredoxin disulfide + H2O
Tequatrovirus T4
-
-
-
-
r
CDP + thioredoxin A
2'-dCDP + thioredoxin A disulfide + H2O
-
-
-
-
?
CDP + thioredoxin A
2'-dCDP + thioredoxin A disulfide + H2O
-
-
-
-
?
CDP + thioredoxin YosR
2'-dCDP + thioredoxin YosR disulfide + H2O
-
-
-
-
?
CDP + thioredoxin YosR
2'-dCDP + thioredoxin YosR disulfide + H2O
-
-
-
-
?
dCDP + DTT disulfide + H2O
CDP + DTT
-
in the assays for the Fe- and Mn-loaded recombinant NrdF, a 10fold excess of recombinant NrdE is used, CDP is the substrate, ATP or dATP is the effector, and DTT is the reductant
-
-
r
dCDP + DTT disulfide + H2O
CDP + DTT
-
in the assays for the Fe- and Mn-loaded recombinant NrdF, a 10fold excess of recombinant NrdE is used, CDP is the substrate, ATP or dATP is the effector, and DTT is the reductant
-
-
r
GDP + thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
-
-
-
?
GDP + thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
-
-
-
-
r
GDP + thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
-
-
-
-
?
GDP + thioredoxin
2'-dGDP + thioredoxin disulfide + H2O
Tequatrovirus T4
-
-
-
-
r
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
at the completion of each turnover cycle, the active site of R1 becomes oxidized and subsequently regenerates by a cysteine pair at its C-terminal domain R1-CTD, that acts in trans to reduce the active site of its neighboring monomer, R1-CTD interacts with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, overview
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
the essential enzyme catalyzes the rate-limiting step in dNTP production for DNA synthesis
-
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
NrdH-redoxin obtained from an overproducing strain, no activity with E. coli thioredoxin
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
possible role in HSV-2-induced transformation
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
CDP, ADP and GDP are reduced very poorly in the absence of allosteric effectors
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
CDP is the only substrate that is reduced with a significant activity even in the absence of allosteric effectors
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
critical and rate-controlling step in pathway leading to DNA synthesis and cell replication
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
thioredoxin is the physiological reductant
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
maximal activity with E. coli thioredoxin
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
dithiothreitol serves as in vitro electron donor, maximal activity with 40 mM
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
in the presence of in vivo concentrations of effectors and all 4 substrates 43% dCDP, 14% dUDP, 31% dADP and 12% dGDP are formed
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
dithiothreitol at higher concentrations i.e. 100 mM can partially substitute for reduced T4 thioredoxin, the rate of CDP reduction is 10% of that obtained with the complete system
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequintavirus T5
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequintavirus T5
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
high concentration of dithiothreitol serves as in vitro hydrogen donor, thioredoxin B of Scenedesmus obliqus and yeast thioredoxin are most effective donors
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
thioredoxin is the physiological reductant
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
dithiothreitol serves as in vitro electron donor, maximal activity with 50-75 mM
-
ir
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
the catalytic reaction in class I RNR involves a long-range electron transfer, coupled to proton transfer, between the substrate binding site in protein R1 and the iron/radical site in protein R2
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
the enzyme catalyses the rate-limiting step of DNA synthesis in the pathogen
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
classical pathway via tyrosyl radical
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
the enzyme catalyses the rate-limiting step of DNA synthesis in the pathogen
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
classical pathway via tyrosyl radical
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
-
-
?
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
-
-
-
-
?
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
-
-
-
-
?
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
-
-
-
ir
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
Tequatrovirus T4
-
-
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
-
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
-
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
-
-
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
-
in the presence of rNrdE, ATP, and CDP, Mn(III)2-Y* and Fe(III)2-Y* rNrdF generate dCDP at rates of 132 and 10 nmol min/mg, respectively
-
-
?
additional information
?
-
-
Bacillus subtilis ribonucleotide reductase can be assayed as a holo-enzyme by using equivalent amounts of each subunit
-
-
?
additional information
?
-
-
in the presence of rNrdE, ATP, and CDP, Mn(III)2-Y* and Fe(III)2-Y* rNrdF generate dCDP at rates of 132 and 10 nmol min/mg, respectively
-
-
?
additional information
?
-
-
Bacillus subtilis ribonucleotide reductase can be assayed as a holo-enzyme by using equivalent amounts of each subunit
-
-
?
additional information
?
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
substrate is CDP, R2 is the catalytic subunit
-
-
?
additional information
?
-
the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview
-
-
?
additional information
?
-
-
the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview
-
-
?
additional information
?
-
-
catalysis by a class I RNR begins when a cysteine residue in the alpha2 subunit is oxidized to a thiyl radical by a cofactor about 35 A away in the beta2 subunit. In a class Ia or Ib RNR, a stable tyrosyl radical is the C oxidant, whereas a MnIV/FeIII cluster serves this function in the class Ic enzyme from Chlamydia trachomatis
-
-
?
additional information
?
-
-
ribonucleotide reduction is the unique step in DNA-precursor biosynthesis and involves radical-dependent redox chemistry and diverse metallo-cofactors, overview. The Mn-RNR from the Gram-positive bacterium Corynebacterium ammoniagenes, strain ATCC 6872, belongs a distinct RNR class IV enzyme
-
-
?
additional information
?
-
-
CDP as substrate
-
-
?
additional information
?
-
-
CDP as substrate
-
-
?
additional information
?
-
-
each catalytic turnover by aerobic ribonucleotide reductase requires the assembly of the two proteins, R1 (alpha2) and R2 (beta2), to produce deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview
-
-
?
additional information
?
-
-
mechanism of radical transport in the R1 subunit of the class I enzyme, overview
-
-
?
additional information
?
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
peroxo-type intermediates occur in the non-heme di-iron enzyme class Ia ribonucleotide reductase. Water or a proton can bind to the di-iron site of ribonucleotide reductase and facilitate changes that affect the electronic structure of the iron sites and activate the site for further reaction. Two potential reaction pathways, spectroscopic and computational analysis, overview
-
-
?
additional information
?
-
-
ribonucleotide reductase catalyzes the reduction of ribonucleotides to deoxyribonucleotides. Electron transfer to and from the tyrosyl radical, at Y122, in RNR is coupled to a conformational change in the beta2 subunit, vibrational spectroscopy analysis, overview
-
-
?
additional information
?
-
the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of nucleoside 5'-diphosphates, NDPs, to deoxynucleotides, dNDPs. The active site for NDP reduction resides in the alpha2 subunit, and the essential diferric-tyrosyl radical, Y122 radical, cofactor that initiates transfer of the radical to the active site cysteine in R2 (C439), 35A ° removed, is located in subunit beta2. The oxidation involves a hopping mechanism through aromatic amino acids, Y122, W48, and Y356 in subunit beta2 to Y731, Y730, and C439 in subunit alpha2, and a reversible proton-coupled electron transfer
-
-
?
additional information
?
-
-
active-site structure and active-site model clusters, overview. Electron transfers and kinetic control, overview
-
-
?
additional information
?
-
-
in the class I RNRs, a tyrosine radical is generated in the beta2 subunit, a di-ironoxo enzyme. In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
additional information
?
-
-
substrate is CDP with ATP as effector, detection of NH2Y radical intermediates capable of dNDP formation
-
-
?
additional information
?
-
-
the class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
additional information
?
-
-
human p53R2 is a 351-residue p53-inducible ribonucleotide reductase small subunit, hp53R2 supplies dNTPs for DNA repair to cells in G0-G1 in a p53-dependent fashion, rather than exhibiting cyclic dNTP synthesis. Hp53R2 structure-function relationship determination and analysis, overview
-
-
?
additional information
?
-
-
CDP as substrate resulting information of product dCDP
-
-
?
additional information
?
-
-
dCDP is produced from CDP by the holoenzyme
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
-
-
?
additional information
?
-
-
the class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of all four ribonucleotides to their corresponding deoxyribonucleotides, the R2 subunit contains a di-iron site, which generates a free radical by the reductive cleavage of molecular oxygen. The free radical is subsequently transferred to the R1 subunit, activating the nucleotide substrate for catalysis
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
the class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
additional information
?
-
-
no substrate activity for L-ribofuranosyl-adenine 5'-diphosphate
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
the class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
additional information
?
-
-
in the class I RNRs, a tyrosine radical is generated in the beta2 subunit, a di-ironoxo enzyme. In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
additional information
?
-
-
DNA damage checkpoints modulate RNR activity through the temporal and spatial regulation of its subunits
-
-
?
additional information
?
-
-
under normal conditions, the cell assembles stoichiometric amounts of tyrosyl radicals essential for enzyme activity per betabeta subunit dimer. Modulation of tyrosyl radical concentration is not involved in regulation of enzyme activity
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
-
-
?
additional information
?
-
-
C-terminus of one monomeric R1 subunit acts in trans to regenerate the active site of its neighboring monomer. The class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
additional information
?
-
-
in the class I RNRs, a tyrosine radical is generated in the beta2 subunit, a di-ironoxo enzyme. In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
GDP + thioredoxin
2'-deoxyGDP + thioredoxin disulfide + H2O
-
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
additional information
?
-
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
the essential enzyme catalyzes the rate-limiting step in dNTP production for DNA synthesis
-
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
possible role in HSV-2-induced transformation
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Herpes simplex virus
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
critical and rate-controlling step in pathway leading to DNA synthesis and cell replication
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
thioredoxin is the physiological reductant
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
Tequatrovirus T4
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
thioredoxin is the physiological reductant
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
the enzyme catalyses the rate-limiting step of DNA synthesis in the pathogen
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
the enzyme catalyses the rate-limiting step of DNA synthesis in the pathogen
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview
-
-
?
additional information
?
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
catalysis by a class I RNR begins when a cysteine residue in the alpha2 subunit is oxidized to a thiyl radical by a cofactor about 35 A away in the beta2 subunit. In a class Ia or Ib RNR, a stable tyrosyl radical is the C oxidant, whereas a MnIV/FeIII cluster serves this function in the class Ic enzyme from Chlamydia trachomatis
-
-
?
additional information
?
-
-
ribonucleotide reduction is the unique step in DNA-precursor biosynthesis and involves radical-dependent redox chemistry and diverse metallo-cofactors, overview. The Mn-RNR from the Gram-positive bacterium Corynebacterium ammoniagenes, strain ATCC 6872, belongs a distinct RNR class IV enzyme
-
-
?
additional information
?
-
-
each catalytic turnover by aerobic ribonucleotide reductase requires the assembly of the two proteins, R1 (alpha2) and R2 (beta2), to produce deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview
-
-
?
additional information
?
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of nucleoside 5'-diphosphates, NDPs, to deoxynucleotides, dNDPs. The active site for NDP reduction resides in the alpha2 subunit, and the essential diferric-tyrosyl radical, Y122 radical, cofactor that initiates transfer of the radical to the active site cysteine in R2 (C439), 35A ° removed, is located in subunit beta2. The oxidation involves a hopping mechanism through aromatic amino acids, Y122, W48, and Y356 in subunit beta2 to Y731, Y730, and C439 in subunit alpha2, and a reversible proton-coupled electron transfer
-
-
?
additional information
?
-
-
human p53R2 is a 351-residue p53-inducible ribonucleotide reductase small subunit, hp53R2 supplies dNTPs for DNA repair to cells in G0-G1 in a p53-dependent fashion, rather than exhibiting cyclic dNTP synthesis. Hp53R2 structure-function relationship determination and analysis, overview
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
DNA damage checkpoints modulate RNR activity through the temporal and spatial regulation of its subunits
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
activity depends on Ca2+
Fe
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Mn(IV)
-
MnIV/FeIII cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Fe2+
-
classIb RNR biferrous site structure, the spectroscopically defined active site contains a 4-coordinate and a 5-coordinate Fe(II), weakly antiferromagnetically coupled via mu-1,3-carboxylate bridges, detailed spectral analysis, overview
Fe2+
-
the isolated recombinant NrdF contains a diferric-tyrosyl radical [Fe(III)2-Y.] cofactor
Fe2+
-
the manganese- and iron content of the R2 subunit decides about the enzyme activity, determination of metal contents, overview
Fe2+
-
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. The R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview. Structure modelling
Fe2+
unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview
Fe2+
-
the enzyme contains only 0.06 mol iron per mol of R2F subunit
Fe2+
each beta-protomer of the small betabeta subunit (R2) contains a binuclear iron cluster with inequivalent binding sites: FeA and FeB. The majority of the protein binds only one Fe(II)atom per betabeta subunit. Additional iron occupation can be achieved upon exposure to O2 or in high glycerol buffers. The binding of the first Fe(II) atom to the active site in a beta-protomer (beta1) induces a global protein conformational change that inhibits access of metal to the active site in the other beta-protomer (betaII). The binding of the same Fe(II) atom also induces a local effect at the active site in beta1-protomer, which lowers the affinity for metal in the A-site
Fe2+
assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview
Fe2+
two Fe2+ ions, each bound to one histidine and one terminal acidic residue, with Asp84 binding to Fe1 and Glu204 binding to Fe2. The di-iron binding site is involved in the catalytic reaction and enzyme activation, overview
Fe2+
-
class Ia ribonucleotide reductase subunit R2 contains a diiron active site, active-site crystal structures of the Fe(II)Fe(II) and Fe(III)Fe(III) clusters, overview
Fe2+
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2
Fe2+
-
monomers A and B exhibit mono- and binuclear iron occupancy, the active site iron coordination environment, involving E131, H134, D100, E194, E228, and H231, is different between monomers A and B, binding structure, overview. Mobility and accessibility of the radical iron center, and radical transfer pathway, overview
Fe3+
-
MnIV/FeIII cofactor
Fe3+
-
class Ia ribonucleotide reductase subunit R2 contains a diiron active site, active-site crystal structures of the Fe(II)Fe(II) and Fe(III)Fe(III) clusters, overview
Fe3+
-
diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
the dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor is 3.5fold more active than the iron form
Iron
-
no stimulation by iron ions
Iron
-
may substitute or manganese
Iron
-
nonheme iron is an essential component of the enzyme
Iron
-
initiator of catalysis is the paramagnetic Fe(III)Fe(IV) state of the iron cluster. Proposition of reaction scheme of the iron site
Iron
-
the class Ic RNR from Chlamydia trachomatis uses a Mn(IV)/Fe(III) cofactor, with high specificity for Mn(IV) in place of the Y for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active Mn(IV)/Fe(III) state, the reduction step in this sequence is mediated by residue Y222, overview
Iron
-
Raman spectroscopy of B2 subunit shows Fe-O vibration of an oxygen-coordinated ligand
Iron
-
iron center stabilizes tyrosyl radical, distance between the iron center and the tyrosyl radical is estimated to be 6-9.0 A
Iron
-
B2 subunit contains 2 nonidentical high spin Fe3+ ions in an antiferromagnetically coupled binuclear complex that resembles both methydroxohemerythrin and oxyhemerythrin
Iron
-
2 separate iron centers in subunit B2, 1 center on each beta subunit, distance between iron centers: 25 A, distance between Fe-Fe atoms: 3.3 A
Iron
proposed in vitro mechanism for the assembly of the diferric tyrosyl radical cofactor of subunit R2
Iron
-
oxo- or carboxylate-bridge between the antiferromagnetically coupled pair of high spin Fe3+, possibly with a binding oxo-group
Iron
-
X-ray absorption fine structure, EXAFS, of iron-containing subunit, Fe-Fe distance in subunit B2 is in the 3.26-3.48 A range
Iron
-
iron binds directly to the enzyme structure and not via sulfur
Iron
-
iron center is composed of 2 high spin iron atoms antiferromagnetically coupled through a micro-oxo bridge
Iron
-
subunit B2 contains iron, nonheme-like porphyrin complexes
Iron
-
B2 subunit contains 2 dinuclear Fe3+ centers
Iron
-
construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites. The binding of the first metal is under kinetic control. The binding of the first Fe(II) atom to the active site in a beta-protomer induces a global protein conformational change that inhibits access of metal to the active site in the other protomer and also induces a local effect at the active site in the first protomer, which lowers the affinity for metal in the A-site
Iron
-
subunit R2 dimer has two equivalent dinuclear iron centers. Iron atoms have both histidine and carboxyl acid ligands and are bridged by the carboxylate group of E115
Iron
-
2 iron atoms and a tyrosyl radical per 88000 Da subunit
Iron
an active diiron-tyrosyl radical cofactor is present in the the R2F-1 small subunit
Iron
-
iron is bound tightly to the protein. Enzyme activity is the same in presence and absence of EDTA
Iron
-
120000 Da L2 subunit of regenerating liver contains iron
Iron
-
1.8 mol of iron per mol of R2F subunit, dinuclear iron center
Iron
Tequatrovirus T4
-
-
Iron
Tequatrovirus T4
-
2.3 atoms of nonheme iron per molecule
Iron
-
no stimulation by iron ions
Manganese
-
dimanganic-tyrosyl radical cofactor
Manganese
-
the class Ic RNR from Chlamydia trachomatis uses a Mn(IV)/Fe(III) cofactor, with high specificity for Mn(IV) in place of the Y for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active Mn(IV)/Fe(III) state, the reduction step in this sequence is mediated by residue Y222, overview
Manganese
-
construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites
Mg2+
-
class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme, with Tyr115. Subunit beta, NrdF, contains the metallo-cofactor, essential for the initiation of the reduction process
Mg2+
-
thymus enzyme: about 50% activity in absence of added Mg2+, optimal Mg2+ concentration varies with concentration of nucleotide effector
Mg2+
-
stimulates CDP but not ADP reduction
Mg2+
-
subunit B1 requires Mg2+ ions in the 10 mM concentration range for activity
Mg2+
-
absolutely required
Mg2+
-
activity depends on Mg2+
Mg2+
Tequatrovirus T4
-
-
Mg2+
Tequatrovirus T4
-
5-10 mM, 2-3fold stimulation, not required for enzyme activity
Mn2+
-
the manganese- and iron content of the R2 subunit decides about the enzyme activity, determination of metal contents, overview
Mn2+
-
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. The R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview. Structure modelling
Mn2+
unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview
Mn2+
EPR-silent Mn bound to the polypeptide chain, approx. 0.5 mol manganese ions/mol of R2F polypeptide
Mn2+
-
R2F is a mangagnese-containing enzyme
Mn2+
-
0.8 mol manganese per mol of R2F subunit, oragnized in a coupled binuclear centre with paramagnetic ground state or in a weakly coupled binuclear centre with therminally populated paramagnetic excites state which appears as binuclear Mn2+, overview
Mn2+
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. Structures of MnII 2-NrdF in complex with reduced and oxidized NrdI: a continuous channel connects the NrdI flavin cofactor to the NrdF MnII 2 active site.
Mn3+
-
dimanganese(III)-tyrosyl radical cofactor
Mn3+
-
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
Mn3+
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
additional information
-
no stimulation by Mg2+ or Fe2+/Fe3+
additional information
-
salt-dependence of calf thymus enzyme: optimal activity in 40 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer, pH 7.6, in the presence of 80-120 mM KCl, precipitation in lower salt concentration, inhibition in higher salt concentration
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
enzyme redox states, overview
additional information
-
R2F does not contain the metals Fe, Co, Ni and Cu
additional information
-
active-site models for the intermediate X-Trp48 radical+ and X-Tyr122 radical, the active Fe(III)Fe(III)-Tyr122 radical, and the met Fe(III)Fe(III) states of Escherichia coli R2 are studied, using broken-symmetry density functional theory incorporated with the conductor-like screening solvation model, overview. Asp84 and Trp48 are most likely the main contributing residues to the result that the transient Fe(IV)Fe(IV) state is not observed in wild-type class Ia R2. Kinetic control of proton transfer to Tyr122 radical plays a critical role in preventing reduction from the active Fe(III)Fe(III)-Tyr122 radical state to the met state, which is potentially the reason why Tyr122 radical in the active state can be stable over a very long period
additional information
Herpes simplex virus
-
Mg2+ is not required for activity in vitro
additional information
-
Glu64 is found in the viral protein in the position that is usually occupied by a metal-coordinating aspartate in other R2s
additional information
-
-
additional information
-
the essential metallo-cofactor is a micro-oxo-micro-carboxylato-diiron cluster adjacent to a stable tyrosyl radical
additional information
-
model of enzyme regulation by nucleoside 5'-triphosphates
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
no stimulation by Mg2+ or Fe2+/Fe3+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-2-(anthracen-9-ylmethylidene)-N-hydroxyhydrazinecarboximidamide
-
i.e. ABNM-13, application leads to significant alterations of deoxyribonucleoside triphosphate pool balance and a highly significant decrease of incorporation of radiolabeled cytidine into DNA of HL-60 cells. Diminished ribonucleotide reductase activity causes replication stress which is consistent with activation of Chk1 and Chk2, resulting in downregulation/degradation of Cdc25A. Cdc25B is upregulated, leading to dephosphorylation and activation of Cdk1. The combined disregulation of Cdc25A and Cdc25B is the most likely cause for ABNM-13 induced S-phase arrest
(E)-2'-fluoromethylene-2'-deoxycytidine-5-diphosphate
-
i.e. N3dNDP, inhibitor forming a furanone intermediate. Modeling of enzyme-inhibitor complex
1-Formylisoquinoline thiosemicarbazone
-
0.0006 mM, 81% inhibition, 0.1 mM desferal reverses inhibition
1-methyl-1-hydroxyurea
-
10 mM, 55% inhibition
2',3'-dideoxy-ATP
-
less potent inhibitor than dATP, 0.1 mM, 50% inhibition of CDP reduction
2'-azido-2'-deoxynucleotides
-
-
2'-chloro-2'-deoxycytidine 5'-diphosphate
-
-
2'-deoxy-2'-azidocytidine diphosphate
2'-halo-2'-deoxynucleotides
-
-
2'-methyladenosine 5'-diphosphate
-
probably mechanism based inhibition, competitive inhibition vs. ADP and GDP
2'-methyluridine 5'-diphosphate
-
probably mechanism based inhibition, competitive inhibition vs. UDP and CDP
2,3,4-Trihydroxybenzamide
-
-
2,3,4-trihydroxybenzohydroxamic acid
2,3-Dihydro-1H-pyrazolo[2,3-a]imidazole
2,3-dihydroxybenzohydroxamic acid
-
0.008 mM, 50% inhibition
2,4-dichlorobenzohydroxamic acid
-
0.45 mM, 50% inhibition
2,4-dihydroxybenzohydroxamic acid
-
0.3 mM, 50% inhibition
2,5-dihydroxybenzohydroxamic acid
-
0.2 mM, 50% inhibition
2,6-dihydroxybenzohydroxamic acid
-
0.1 mM, 50% inhibition
2-(diphenylmethylidene)-N,N-dimethylhydrazinecarbothioamide
-
metal chelator, significantly decreases ribonucleotide reductase activity, whereas the NADPH/NADP+ total ratio is not reduced
2-acetylpyridine N,N-dimethylthiosemicarbazonato-N,N,S-dichlorogallium(III)
-
-
2-acetylpyridine N-pyrrolidinylthiosemicarbazonato-N,N,S-dichlorogallium(III)
-
-
2-aminobenzohydroxamic acid
-
0.12 mM, 50% inhibition
2-azido-UDP
-
rapid time dependent inactivation
2-furan-3-ylbenzaldehyde N-(4-hydroxyphenyl)thiosemicarbazone
-
-
2-furan-3-ylbenzaldehyde N-phenylthiosemicarbazone
-
-
2-hydroxy-3-methylbenzohydroxamic acid
-
0.15 mM, 50% inhibition
2-hydroxy-4-aminobenzohydroxamic acid
-
0.2 mM, 50% inhibition
2-hydroxybenzaldehyde N-(4-chlorophenyl)thiosemicarbazone
-
-
2-hydroxybenzaldehyde N-phenylthiosemicarbazone
-
-
2-hydroxybenzohydroxamic acid
-
0.15 mM, 50% inhibition
2-Nitro-imidazole
-
trivial name azomycin
2-thiophen-2-ylbenzaldehyde N-(4-chlorophenyl)thiosemicarbazone
-
-
2-thiophen-2-ylbenzaldehyde N-phenylthiosemicarbazone
-
-
2-[di(pyridin-2-yl)methylidene]-N,N-dimethylhydrazinecarbothioamide
-
metal chelator, significantly decreases ribonucleotide reductase activity, whereas the NADPH/NADP+ total ratio is not reduced
3,4,5-Trihydroxybenzamide
-
-
3,4,5-Trihydroxybenzohydroxamic acid
3,4,5-Trihydroxybenzoic acid
-
-
3,4,5-trimethoxybenzohydroxamic acid
-
0.1 mM, 50% inhibition
3,4-diaminobenzohydroxamic acid
-
0.04 mM, 50% inhibition
3,4-dichlorobenzohydroxamic acid
-
0.3 mM, 50% inhibition
3,4-Dihydroxybenzamide
-
-
3,4-dihydroxybenzohydroxamic acid
3,4-dimethoxybenzohydroxamic acid
-
0.3 mM, 50% inhibition
3,4-dimethylbenzohydroxamic acid
-
0.3 mM, 50% inhibition
3,5-diamino-1H-1,2,4-triazole
3,5-diaminopyridine-2-carboxaldehyde thiosemicarbazone
-
-
3,5-dihydroxybenzohydroxamic acid
-
0.4 mM, 50% inhibition
3-amino-4-methylpyridine-2-carboxaldehyde thiosemicarbazone
-
-
3-aminobenzohydroxamic acid
-
0.35 mM, 50% inhibition
3-aminopyridine-2-carboxaldehyde thiosemicarbazone
3-aminopyridine-2-carboxaldehyde-thiosemicarbazone
-
i.e. 3-AP, phase I study in combination with high dose cytarabine in patients with advanced myeloid leukemia, resulting in enhanced cytarabine cytotoxicity with possible methemoglobinemia, overview
3-hydroxybenzohydroxamic acid
-
0.35 mM, 50% inhibition
3-methyl aminopyridine-2-carboxaldehyde thiosemicarbazone
-
-
3-methyl-1-hydroxyurea
-
10 mM, 57% inhibition
3-Methyl-4-nitrophenol
-
-
4-Amino-2-phenylimidazole-5-carboxamide
-
-
4-aminobenzohydroxamic acid
-
0.15 mM, 50% inhibition
4-dimethylaminobenzohydroxamic acid
-
0.5 mM, 50% inhibition
4-hydroxy-3-methoxybenzaldehyde N-(4-chlorophenyl)thiosemicarbazone
-
-
4-hydroxy-3-methoxybenzaldehyde N-phenylthiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(2-chlorophenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(2-hydroxyphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(2-methoxyphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(2-methylphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(2-nitrophenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(3-chlorophenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(3-hydroxyphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(3-methylphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(4-chlorophenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(4-hydroxyphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(4-methylphenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-(4-nitrophenyl)thiosemicarbazone
-
-
4-hydroxybenzaldehyde N-phenylthiosemicarbazone
-
-
4-hydroxybenzohydroxamic acid
-
0.30 mM, 50% inhibition
4-methoxybenzohydroxamic acid
-
0.5 mM, 50% inhibition
4-Methyl-5-amino isoquinoline-1-carboxaldehyde thiosemicarbazone
4-Methyl-5-amino-1-formylisoquinoline thiosemicarbazone
4-methylaminobenzohydroxamic acid
-
0.33 mM, 50% inhibition
4-nitrobenzohydroxamic acid
-
0.5 mM, 50% inhibition
5'-O-valproyl-3'-C-methyladenosine
inhibits ribonucleotide reductase activity by competing with ATP as an allosteric effector and concomitantlyreduces the intracellular deoxyribonucleoside triphosphate pools. In contrast to previously used ribonucleotide reductase nucleoside analogs does not require intracellular kinases for its activity and therefore holds promise against drug resistant tumors with downregulated nucleoside kinases
-
5-(1-Aziridinyl)-2,4-dinitrobenzamide
5-amino-4-morpholinomethylpyridine-2-carboxaldehyde thiosemicarbazone
-
-
5-aminopyridine-2-carboxaldehyde thiosemicarbazone
-
-
5-hydroxy-4-methyl-1-formylisoquinoline thiosemicarbazone
-
-
5-methyl-4-amino-1-formylisoquinoline thiosemicarbazone
-
-
6-chloro-9H-(3-C-methyl-2,3-di-O-acetyl-5-O-benzoyl-beta-D-ribofuranosyl)purine
-
-
8-hydroxyquinoline 5-sulfonate
bathophenanthroline disulfonate
bathophenanthroline sulfonate
benzohydroxamic acid
-
0.4 mM, 50% inhibition
butylphenyl-dGTP
-
0.13 mM, 50% inhibition of ADP reduction
Catechol derivatives
-
-
-
clofarabine
-
an adenosine analogue is used in the treatment of refractory leukemias. Its mode of cytotoxicity is associated in part with the triphosphate functioning as an allosteric reversible inhibitor of hRNR, rapid inactivation
clofarabine diphosphate
-
ClFDP, a C-site slow-binding, reversible inhibitor, mechanism of inhibition via altering the quaternary structure of the large subunit of RNR, overview. Binds also mutant D57N-alpha subunit. CDP protects against inhibition
clofarabine triphosphate
-
ClFTP, an A-site rapidly binding reversible inhibitor, mechanism of inhibition via altering the quaternary structure of the large subunit of RNR, overview. Neither CDP (C site) nor dGTP (A site) had any effect on inhibition by ClFTP
dADP
-
product inhibition
dCDP
-
product inhibition
dGDP
-
product inhibition
dithiothreitol
-
higher than 10 mM, activation below
dITP
-
inhibition of CDP reduction
dUDP
-
product inhibition
dUTP
-
inhibition of: CDP reduction, UDP reduction
ethyleneglycol-bis-(2-aminoethylether)-N,N,N',N'-tetraacetic acid
-
trivial name EGTA
Fmoc(NCH3)PhgLDChaDF
-
inhibitor identified by competition with inhibitor N-AcFTLDADF and inhibition of enzyme activity
FmocWFDF
-
inhibitor identified by competition with inhibitor N-AcFTLDADF and inhibition of enzyme activity
FmocWVFF
-
inhibitor identified by competition with inhibitor N-AcFTLDADF and inhibition of enzyme activity
formohydroxamic acid
-
10 mM, 43% inhibition
FTLDADF
-
last seven amino acid residues of carboxyl terminus of the R2 subunit of mouse enzyme and its N-alpha-acetyl derivative inhibit thymus enzyme
gamma-L-Glutaminyl-4-hydroxybenzene
-
naturally occuring quinol from spores of Agaricus bisporus, 0.76 mM, 50% inhibition
glutaminyl-3,4-dihydroxybenzene
-
1.23 mM, 50% inhibition
glutathione
-
analogs with aromatic substituents
H2O2
-
0.01%, 81% inhibition
hydroxylamine
-
10 mM, complete inhibition
IRBIT
IRBIT is a conserved metazoan protein implicated in diverse functions. IRBIT consists of a putative enzymatic domain that has similarity to S-adenosylhomocysteine hydrolase and an essential N-terminal domain of 104 amino acids. It forms a dATPdependent complex with ribonucleotide reductase, which stabilizes dATP in the activity site of ribonucleotide reductase and thus inhibits the enzyme. Formation of the ribonucleotide reductase-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression. Under normal physiological conditions, where ATP levels are high, such inhibition can only be achieved when binding of IRBIT is strengthened by phosphorylation
-
Isoquinoline-1-carboxaldehyde thiosemicarbazone
L-ADP
-
inhibition of D-ADP reduction, competitive inhibition of dGTP-dependent D-ADP reductase
mammalian R2 C-terminal heptapeptide P7
Ac-1FTLDADF7, the inhibitor binds at bind at a contiguous site containing residues that are highly conserved among eukaryotes, binding structure, overview
meso-alpha,beta-Diphenylsuccinate
-
-
Methyl 3,4,5-trihydroxybenzoate
-
-
monoclonal antibody raised against yeast tubulin
-
CDP reductase activity is inhibited to a greater extent than ADP, UDP or GDP reductase activity, antibody recognizes a specific sequence in the C-terminal region on the R2 subunit
-
N,2,3,4-tetrahydroxybenzamide
-
0.012 mM, 50% inhibition, reversible
N-AcFTLDADF
-
heptapeptide inhibitor based on subunit R2 C-terminus
N-alpha-acetyl-FTLDADF
-
-
N-ethylmaleimide
-
0.1 mM, 50% inhibition of intact enzyme, 0.05 mM, 50% inhibition of effector-binding subunit, 0.3 mM, 50% inhibition of non-heme iron subunit
n-Hexanohydroxamic acid
-
-
N-Hydroxy-alpha-aminoheptanoate
-
5 mM, 50% inhibition
N-Hydroxy-alpha-aminohexanoate
-
15 mM, 50% inhibition
N-hydroxyguanidine
-
10 mM, 89% inhibition
N-hydroxyurethane
-
10 mM, 66% inhibition
N-Methyl 3,4,5-trihydroxybenzamide
-
-
N-[[(3S,5S,7S,7aS)-7-([[3-(9H-fluoren-9-yl)propanoyl]oxy]methyl)-3-hydroxy-5-(2-methylpropoxy)hexahydropyrano[3,4-b]pyrrol-1(2H)-yl]acetyl]-L-alpha-aspartyl-L-phenylalanine
-
50% inhibition at 0.04-0.05 mM, bicyclic scaffold is necessary to maintain inhibitory activity
N6-(2-furanylmethyl)-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-(2-thienylmethyl)-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-(3-pyrazolyl)-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-cyclobutyl-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-cycloheptyl-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-endo-norbonyl-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
N6-phenyl-9H-(3-C-methyl-beta-D-ribofuranosyl)adenine
-
-
nicotinohydroxamic acid
-
0.8 mM, 50% inhibition
NSFTLDADF
-
inhibition of CDP reductase activity, peptide corresponds to the C-terminal region of the R2 subunit and competes with binding of R2 to the R1 subunit
nucleotide analogs
-
overview
-
o-ClBzocFc[ELDK]DF
-
inhibitor identified by competition with inhibitor N-AcFTLDADF and inhibition of enzyme activity
p-chloromercuribenzoate
-
0.35 mM, 50% inhibition of intact enzyme, 0.15 mM, 50% inhibition of effector-binding subunit, 1.5 mM, 50% inhibition of non-heme iron subunit
peptide P6
1Fmoc(Me)PhgLDChaDF7, the inhibitor binds at a contiguous site containing residues that are highly conserved among eukaryotes. The Fmoc group in P6 peptide forms several hydrophobic interactions that contribute to its enhanced potency in binding to ScR1, binding structure, overview
peptide Y-R2C19
-
a 20-mer peptide, which is identical to the C-terminal peptide tail of the R2 subunit and is a known competitive inhibitor of binding of the native R2 protein to R1
-
Periodate-oxidized inosine
-
phenylacetohydroxamic acid
-
1 mM, 50% inhibition
picolinohydroxamic acid
-
0.5 mM, 50% inhibition
Polyhydroxybenzohydroxamic acid
-
Pyridine-2-carboxaldehyde thiosemicarbazone
pyridoxal 5'-phosphate
Herpes simplex virus
-
1 mM, 65% inhibition, 3 mM, 90% inhibition
pyridoxal 5'-phosphate/NaBH4
-
-
Pyrogallol derivatives
-
-
-
quercetin
-
i.e. 3,3',4',5,7-pentahydroxyflavone, isolated from air-dried powdered leaves of Vitex negundo, a lipophilic metal chelator, that interferes with the parasite's iron metabolism inhibiting Fe2+ acquisition from an endogenous source, combination of quercetin with serum albumin increases its bioavailability, the inhibitor causes deprivation of the enzyme of iron which in turn destabilized the critical tyrosyl radical required for its catalysing activity
Sml1
-
inhibitor protein Sml1 competes with the C-terminal domain of subunit R1 for association with its N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle
-
Sml1 protein
-
a 104-residue Saccharomyces cerevisiae protein, inhibits ribonucleotide reductase activity by binding to the R1 subunit interacting with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, the Sml1-R1 interaction causes SML1-dependent lethality, overview
-
sodium arsenite
-
0.025 mM, almost complete inhibition of CDP reduction, 86% inhibition of GDP reduction
Synthetic peptides
-
which specifically inhibit the activity of virus-induced enzyme
-
YAGAVVNDL
Herpes simplex virus
-
peptide may prevent association of the two subunits by competing for the subunit binding site
YGAVVNDL
Herpes simplex virus
-
-
[bis(2-acetylpyridine N,N-dimethylthiosemicarbazonato)-N,N,S-gallium(III)] hexafluorophosphate
-
-
[bis(2-acetylpyridine N,N-dimethylthiosemicarbazonato)-N,N,S-iron(III)] hexafluorophosphate
-
-
[bis(2-acetylpyridine N,N-dimethylthiosemicarbazonato)-N,N,S-iron(III)] tetrachloroferrate(III)
-
-
[bis(2-acetylpyridine N-pyrrolidinylthiosemicarbazonato)-N,N,S-gallium(III)] hexafluorophosphate
-
-
[bis(2-acetylpyridine N-pyrrolidinylthiosemicarbazonato)-N,N,S-iron(III)] hexafluorophosphate
-
-
[bis(2-acetylpyridine N-pyrrolidinylthiosemicarbazonato)-N,N,S-iron(III)] tetrachloroferrate(III)
-
-
[bis(acetylpyrazine N,N-dimethylthiosemicarbazonato)-N,N,S-gallium(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N,N-dimethylthiosemicarbazonato)-N,N,S-iron(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N,N-dimethylthiosemicarbazonato)-N,N,S-iron(III)] tetrachloroferrate(III)
-
-
[bis(acetylpyrazine N-piperidinylthiosemicarbazonato)-N,N,S-gallium(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N-piperidinylthiosemicarbazonato)-N,N,S-iron(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N-piperidinylthiosemicarbazonato)-N,N,S-iron(III)] tetrachloroferrate(III)
-
-
[bis(acetylpyrazine N-pyrrolidinylthiosemicarbazonato)-N,N,S-gallium(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N-pyrrolidinylthiosemicarbazonato)-N,N,S-iron(III)] hexafluorophosphate
-
-
[bis(acetylpyrazine N-pyrrolidinylthiosemicarbazonato)-N,N,S-iron(III)] tetrachloroferrate(III)
-
-
[FeCl4] 2-acetylpyridine N,N-dimethylthiosemicarbazone
-
Ga(III) and Fe(III) complexes destroy the tyrosyl radical of the presumed target ribonucleotide reductase
[FeCl4] 2-acetylpyridine N-pyrrolidinylthiosemicarbazone
-
-
[FeCl4] acetylpyrazine N,N-dimethylthiosemicarbazone
-
-
[FeCl4] acetylpyrazine N-piperidinylthiosemicarbazone
-
-
[FeCl4] acetylpyrazine N-pyrrolidinylthiosemicarbazone
-
-
[GalCl2] 2-acetylpyridine N,N-dimethylthiosemicarbazone
-
Ga(III) and Fe(III) complexes destroy the tyrosyl radical of the presumed target ribonucleotide reductase
[GalCl2] 2-acetylpyridine N-pyrrolidinylthiosemicarbazone
-
-
[GalCl2] acetylpyrazine N,N-dimethylthiosemicarbazone
-
-
[GalCl2] acetylpyrazine N-piperidinylthiosemicarbazone
-
-
[GalCl2] acetylpyrazine N-pyrrolidinylthiosemicarbazone
-
-
(-)-epicatechin
-
interacts with the R2 protein, leading to a loss of the tyrosyl radical EPR signal. Proliferation of cells exposed to (-)-epicatechin is downregulated, and deoxyribonucleotide levels are significantly diminished
(-)-epicatechin
-
interacts with the R2 protein, leading to a loss of the tyrosyl radical EPR signal. Proliferation of cells exposed to (-)-epicatechin is downregulated, and deoxyribonucleotide levels are significantly diminished
1,10-phenanthroline
-
-
1,10-phenanthroline
Tequatrovirus T4
-
-
1,10-phenanthroline
-
0.2 mM, 50% inhibition
2'-deoxy-2'-azidocytidine diphosphate
-
thymus enzyme, reversible inhibition
2'-deoxy-2'-azidocytidine diphosphate
-
inactivation
2,3,4-trihydroxybenzohydroxamic acid
-
0.009 mM, 50% inhibition, reversible
2,3,4-trihydroxybenzohydroxamic acid
-
0.0035 mM, 50% inhibition
2,3,4-trihydroxybenzohydroxamic acid
-
0.012 mM, 50% inhibition, hydroxyurea-resistant cells
2,3-Dihydro-1H-pyrazolo[2,3-a]imidazole
Herpes simplex virus
-
noncompetitive vs. CDP
2,3-Dihydro-1H-pyrazolo[2,3-a]imidazole
-
-
2,3-Dihydro-1H-pyrazolo[2,3-a]imidazole
-
mechanism of inhibition
3,4,5-Trihydroxybenzohydroxamic acid
-
-
3,4,5-Trihydroxybenzohydroxamic acid
-
0.01 mM, 50% inhibition
3,4-dihydroxybenzohydroxamic acid
-
0.033 mM, 50% inhibition, reversible
3,4-dihydroxybenzohydroxamic acid
-
2.5 mM, 50% inhibition
3,4-dihydroxybenzohydroxamic acid
-
0.03 mM, 50% inhibition
3,4-dihydroxybenzohydroxamic acid
Tequatrovirus T4
-
0.3 mM, 50% inhibition
3,5-diamino-1H-1,2,4-triazole
-
trivial name guanazole
3,5-diamino-1H-1,2,4-triazole
-
0.001 mM, 50% inhibition of CDP and UDP reduction, 0.05 mM, 50% inhibition of ADP reduction
3,5-diamino-1H-1,2,4-triazole
Herpes simplex virus
-
noncompetitive vs. CDP; trivial name guanazole
3,5-diamino-1H-1,2,4-triazole
-
trivial name guanazole
3,5-diamino-1H-1,2,4-triazole
-
-
3,5-diamino-1H-1,2,4-triazole
-
2.3 mM, 50% inhibition of CDP reduction, 2.6 mM, 50% inhibition of ADP reduction
3,5-diamino-1H-1,2,4-triazole
-
trivial name guanazole
3,5-diamino-1H-1,2,4-triazole
-
2 mM, 41% inhibition, presence of 0.1 mM desferal potentiates inhibition; trivial name guanazole
3,5-diamino-1H-1,2,4-triazole
-
trivial name guanazole
3-aminopyridine-2-carboxaldehyde thiosemicarbazone
-
i.e.3-AP or triapine, in combination with the nucleoside analog fludarabine for patients with refractory acute leukemias and aggressive myeloprol, phase I study, detailed overview, the inhibitor inhibits the M2 subunit, and depletes intracellular deoxyribonculeotide pools, especially dATP
3-aminopyridine-2-carboxaldehyde thiosemicarbazone
-
triapine
4-Methyl-5-amino isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
4-Methyl-5-amino isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
4-Methyl-5-amino isoquinoline-1-carboxaldehyde thiosemicarbazone
-
inhibits the non-heme iron subunit
4-Methyl-5-amino isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
4-Methyl-5-amino-1-formylisoquinoline thiosemicarbazone
Herpes simplex virus
-
inactivation, half-life: 3 min
4-Methyl-5-amino-1-formylisoquinoline thiosemicarbazone
-
0.0003 mM, 93% inhibition, 0.1 mM desferal reverses inhibition
4-Methyl-5-amino-1-formylisoquinoline thiosemicarbazone
-
-
5-(1-Aziridinyl)-2,4-dinitrobenzamide
-
-
5-(1-Aziridinyl)-2,4-dinitrobenzamide
-
-
8-hydroxyquinoline
-
-
8-hydroxyquinoline 5-sulfonate
-
-
8-hydroxyquinoline 5-sulfonate
-
-
8-hydroxyquinoline 5-sulfonate
-
no inhibition in the presence of excess iron
8-hydroxyquinoline 5-sulfonate
-
-
Acetohydroxamic acid
-
-
Acetohydroxamic acid
-
1 mM, 50% inhibition
ADP
Herpes simplex virus
-
competitive inhibition of CDP reduction
ATP
Herpes simplex virus
-
free ATP, 0.32 mM, 50% inhibition
ATP
Herpes simplex virus
-
3 mM, 65% inhibition
ATP
-
CDP reduction is inhibited by free ATP
ATP
-
4 mM, 50% inhibition of GDP reduction in the presence of dTTP
aurintricarboxylate
-
oligomeric form
aurintricarboxylate
-
oligomeric form
aurintricarboxylate
-
oligomeric form
aurintricarboxylate
-
0.005 mM, 50% inhibition; oligomeric form
bathophenanthroline disulfonate
-
-
bathophenanthroline disulfonate
-
-
bathophenanthroline disulfonate
-
-
bathophenanthroline sulfonate
-
1.5 mM, complete inactivation after 30 min, complete reactivation with FeCl3
bathophenanthroline sulfonate
-
5 mM, almost complete inhibition of CDP and GDP reduction
bathophenanthroline sulfonate
-
no effect in the presence of excess iron
caracemide
-
-
CDP
-
competitive inhibition of UDP reduction
CDP
Herpes simplex virus
-
competitive inhibition of ADP reduction
chlorambucil
-
-
cisplatin
-
more than 90% irreversible inhibition by inhibitor/enzyme ratios smaller than 2 under anaerobic conditions, 0.4 mM, 50% inhibition under aerobic conditions, inhibition of B1 subunit
Co2+
-
RNR activity chelates with copper leading to inactivation
Co2+
-
RNR activity chelates with copper leading to inactivation
Co2+
-
RNR activity chelates with copper leading to inactivation
Co2+
-
RNR activity chelates with copper leading to inactivation
Co2+
-
RNR activity chelates with copper leading to inactivation
dATP
-
inhibition of CDP reduction
dATP
-
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP
-
inhibition of CDP reduction in the presence of ATP
dATP
-
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
-
inhibition of ADP reduction
dATP
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
-
inhibition of CDP reduction; inhibition of UDP reduction
dATP
-
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
dATP
-
inhibition by dATP has a regulatory function
dATP
-
inhibition of ADP reduction
dATP
Herpes simplex virus
-
HSV type 2, 1 mM, 20% inhibition
dATP
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
-
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
dATP
-
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
dATP
-
inhibition of CDP, UDP, GDP and ADP reduction
dATP
-
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
dATP
-
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
dATP
-
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
dATP
-
0.05 mM, 10% residual activity
dATP
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
-
inhibition of CDP reduction
dATP
-
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
dATP
-
inhibition by dATP has a regulatory function
dATP
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
dATP
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
-
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
dATP
-
inhibition by dATP has a regulatory function
dATP
Tequatrovirus T4
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
dATP
Tequatrovirus T4
-
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
dATP
Tequintavirus T5
-
inhibition of ADP reduction
dATP
-
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
dCTP
-
1.2 mM, 50% inhibition of CDP reduction, 0.89 mM, 50% inhibition of ADP reduction
dCTP
-
1 mM, 50% inhibition of CDP reduction
deferoxamine mesylate
-
IC50 for subunit p53R2 is 0.00316 mM, IC50 for hRRM2 subunit is 0.5 mM
deferoxamine mesylate
-
an iron chelator
dGTP
-
0.05 mM, 50% inhibition of GDP reduction; 0.1 mM, 50% inhibition of CDP and UDP reduction; inhibition of UDP reduction
dGTP
-
1.2 mM, 50% inhibition of CDP reduction, 0.93 mM, 50% inhibition of ADP reduction
dGTP
-
0.08 mM, 50% inhibition of CDP reduction, 0.19 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
dGTP
-
inhibition of GDP reduction
dGTP
-
0.1 mM, 12% residual activity
dGTP
-
inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
dGTP
-
inhibition of UDP reduction
dGTP
Tequatrovirus T4
-
inhibition of ATP- and dATP stimulated CDP reduction
dGTP
Tequatrovirus T4
-
-
dGTP
Tequintavirus T5
-
-
dTTP
-
inhibition of CDP reduction
dTTP
-
inhibition of UDP reduction
dTTP
-
inhibition of ADP reduction
dTTP
Herpes simplex virus
-
HSV type 2, 1 mM, 20% inhibition
dTTP
-
inhibition of CDP reduction
dTTP
-
0.2 mM, 50% inhibition of CDP reduction
dTTP
-
inhibition of ADP- CDP- and UDP reduction
dTTP
-
inhibition of CDP reduction
dTTP
-
inhibition of CDP reduction; inhibition of UDP reduction
dTTP
-
inhibition of UDP reduction
dTTP
Tequatrovirus T4
-
-
dTTP
Tequintavirus T5
-
-
dTTP
-
inhibition of CDP reduction
EDTA
-
-
EDTA
-
reversible stimulation of GDP reduction, irreversible inhibition of CDP reduction
EDTA
-
1 mM, 72% inhibition
EDTA
-
10 mM, 50% inhibition
Fe2+
-
-
Fe2+
-
no effect of iron salts
Fe2+
-
concentrations higher than 0.1-1 mM
Fe2+
-
0.2 mM, 50% inhibition
GDP
-
-
gemcitabine
-
i.e. F2dNDP, inhibitor forming a furanone intermediate. Modeling of enzyme-inhibitor complex
Hydroxyurea
-
-
Hydroxyurea
-
1 mM, complete inactivation of thymus enzyme
Hydroxyurea
-
1 mM, approx. 90% inhibition; thymus enzyme, reversible inhibition
Hydroxyurea
-
inhibition of the enzyme by the 1-electron donor hydroxyurea produces the Mn(III)Fe(III) state
Hydroxyurea
-
inactivates both Ia/b and Ic beta2 subunits by reducing their C oxidants, reacts with the MnIV/FeIII cofactor to give two distinct products: the homogeneous MnIII/FeIII-beta2 complex, which forms only under turnover conditions, in the presence of alpha2 and the substrate, and a distinct, diamagnetic Mn/Fe cluster, which forms about 900fold less rapidly as a second phase in the reaction under turnover conditions and as the sole outcome in the reaction of MnIV/FeIII-beta2 only
Hydroxyurea
2 mM, approx. 80% inactivation
Hydroxyurea
-
10 mM, complete inhibition, 0.3 mM, 50% inhibition
Hydroxyurea
-
0.5 mM, 50% inhibition
Hydroxyurea
-
IC50 for subunit p53R2 is 2.48 mM, IC50 for hRRM2 subunit is 0.991 mM
Hydroxyurea
-
inhibits the M2 subunit
Hydroxyurea
-
1 mM, 98 and 81% inhibition of CDP and GDP reduction respectively
Hydroxyurea
-
2 mM, 93% inhibition, presence of 0.1 mM desferal potentiates inhibition
Hydroxyurea
-
inhibits the non-heme iron subunit; mechanism of inhibition
Hydroxyurea
wild-type plants exposed to a low concentration of an RNR inhibitor, hydroxyurea, produce chlorotic leaves without growth retardation, reminiscent of v3 and st1 mutants; wild-type plants exposed to a low concentration of an RNR inhibitor, hydroxyurea, produce chlorotic leaves without growth retardation, reminiscent of v3 and st1 mutants
Hydroxyurea
-
approx. 0.5 mM, 50% inhibition
Hydroxyurea
Tequatrovirus T4
-
0.025 mM, 50% inhibition
Hydroxyurea
Tequatrovirus T4
-
-
Hydroxyurea
Tequatrovirus T4
-
0.01-0.03 mM, 50% inhibition, 0.2 mM, complete inhibition
Hydroxyurea
Tequintavirus T5
-
-
Hydroxyurea
-
1.5 mM, 50% inhibition
Isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
Isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
Isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
Isoquinoline-1-carboxaldehyde thiosemicarbazone
-
-
Mg2+
Herpes simplex virus
-
uncomplexed Mg2+, 3.7 mM, 50% inhibition
Mg2+
-
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
Mg2+
-
2 mM, 50% inhibition
Mn2+
-
concentrations higher than 0.1-1 mM
Mn2+
-
0.2 mM, 50% inhibition
N-Methylhydroxylamine
-
10 mM, 94% inhibition
N-Methylhydroxylamine
-
-
Periodate-oxidized inosine
Herpes simplex virus
-
inactivation, 1 mM, half-life: 6 min
-
Periodate-oxidized inosine
-
-
-
Polyhydroxybenzohydroxamic acid
-
-
-
Polyhydroxybenzohydroxamic acid
-
-
-
Polyhydroxybenzohydroxamic acid
Tequatrovirus T4
-
-
-
pyrazoloimidazol
-
2 mM, 79% inhibition, presence of 0.1 mM desferal potentiates inhibition, inhibits the non-heme iron subunit
Pyridine-2-carboxaldehyde thiosemicarbazone
-
-
Pyridine-2-carboxaldehyde thiosemicarbazone
-
-
Pyridine-2-carboxaldehyde thiosemicarbazone
-
-
Pyridine-2-carboxaldehyde thiosemicarbazone
-
-
Thenoyltrifluoroacetone
-
5 mM, almost complete inhibition of CDP and GDP reduction
Thenoyltrifluoroacetone
-
-
triapine
-
IC50 for subunit p53R2 is 112 nM, IC50 for hRRM2 subunit is 144 nM
triapine
-
i.e. 3-AP, triapine enhances the cytotoxicity of gemcitabine and arabinoside cytosine in four non-small-cell-lung-cancer cell lines, e.g. in SW1573 cells, but not in H460 cells, multiple-drug-effect analysis, overview
UDP
-
competitive inhibition of CDP reduction
UDP
-
inhibition of CDP reduction
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
the enzyme is inhibited by radical scavengers
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
overview
-
additional information
-
mechanism-based inhibitors
-
additional information
-
8-vinyl-ADP is efficiently reduced. The anti-tumoral and anti-viral activity of 8-vinyladenosine can unlikely result from inhibition of ribonucleotide diphosphate reductase
-
additional information
-
reaction involves formation of a keto-deoxyribonucleotide intermediate. In case of furanone inhibitors, the intermediate dissociates from the active site, depending on the solvation free energy of the 2-substituents, its influence inside the active site, and the charge transfer mechanism from a protein side chain to solution as thermodynamic driving forces. Substrates do not dissociate from the active site but complete the catalytic cycle
-
additional information
Herpes simplex virus
-
enzyme does not respond to feedbck inhibition by dTTP or dATP
-
additional information
Herpes simplex virus
-
mechanism studied with inhibitors
-
additional information
Herpes simplex virus
-
-
-
additional information
Herpes simplex virus
-
-
-
additional information
Herpes simplex virus
-
not inhibited by dATP and dTTP
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
no enzyme inhibition by arabinoside cytosine
-
additional information
-
synthesis, characterization, cytotoxicity in human cell lines, and interaction with ribonucleotide reductase of gallium(III) and iron(III) complexes of alpha-N-heterocyclic thiosemicarbazones, overview, gallium(III) enhances, whereas iron(III) weakens the cytotoxicity of the ligands
-
additional information
-
construction and synthesis of ribose-modified purine nucleosides as ribonucleotide reductase inhibitors. Synthesis, antitumor activity, and molecular modeling of N6-substituted 3-C-methyladenosine derivatives, an unsubstituted N6-amino group is essential for optimal cytotoxicity of 3'-Me-Ado. The anticancer nucleosides act as antimetabolites after metabolic activation by phosphorylation to the corresponding 5'-di- or 5'-triphosphates, overview
-
additional information
-
inhibitory mechanisms of heterocyclic carboxaldehyde thiosemicabazones
-
additional information
-
synthesis and ribonucleotide reductase inhibitory activity of thiosemicarbazones, overview
-
additional information
-
each ribonucleoside diphosphate substrate is competitively inhibited by reduction of each other substrate
-
additional information
-
-
-
additional information
-
inhibition of reductase by hydroxyurea, guanazole and pyrazolo-imidazole is potentiated by iron-chelating agents e.g. EDTA, desferrioxamine mesylate and 8-hydroxyquinoline, inhibition by 4-methyl-5-amino-1-formylisoquinoline thiosemicarbazone and 1-formylisoquinoline thiosemicarbazone is reversed by iron chelating agents
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
L1210 cells with resistance to specific nucleotide reductase inhibitors
-
additional information
-
-
-
additional information
-
comprehensive and quantitative model for allosteric control of mRR enzymatic activity based on molecular mass, ligand binding and enzyme activity studies
-
additional information
-
synthesis, characterization, and interaction with ribonucleotide reductase subunit R2 of gallium(III) and iron(III) complexes of alpha-N-heterocyclic thiosemicarbazones, overview, gallium(III) enhances, whereas iron(III) weakens the cytotoxicity of the ligands
-
additional information
-
synthesis and evaluation of peptide inhibitors of RNR derived from the C-terminus of the small subunit of Mycobacterium tuberculosis RNR, based on the heptapeptide Ac-Glu-Asp-Asp-Asp-Trp-Asp-Phe-OH with Trp5 and Phe7 being very important for inhibitory potency, overview
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
not inhibitory: EDTA
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
not inhibited by 8-hydroxyquinoline and o-phenanthroline
-
additional information
Tequatrovirus T4
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
25 mM, maximal activation, 70% of activity with dithiothreitol
adenyl-5'-yl-imidodiphosphate
dGDP
-
40% less effective than dGTP
dihydrolipoic acid
-
slight stimulation
dithioerythritol
-
0.5 mM, maximal activation, 94% of activity with dithiothreitol
dITP
-
activation of ADP reduction
E. coli thioredoxin reductase
-
EDTA
-
reversible stimulation of GDP reduction, irreversible inhibition of CDP reduction
GTP
-
stimulation of CDP and ADP reduction
O2
-
activates the MnIV/FeIII cofactor, overview
P1,P4-bis(5'-adenosyl) tetraphosphate
-
stimulation at low concentrations, inhibition above 0.3 mM
P53
-
activates, required
thioredoxin reductase
Tequatrovirus T4
-
Escherichia coli enzyme
-
TTP
the binding of effector TTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
adenyl-5'-yl-imidodiphosphate
-
maximal activation of CDP reduction at 4 mM
adenyl-5'-yl-imidodiphosphate
-
can replace ATP as activator of CDP and UDP reduction
adenyl-5'-yl-imidodiphosphate
-
stimulation at low concentration, inhibition above 0.3 mM
ATP
-
stimulation of CDP reduction
ATP
-
ATP maximally stimulates CDP reduction at 1.5 mM
ATP
-
stimulation of UDP reduction
ATP
-
stimulation of CDP reduction
ATP
stimulation of CDP reduction
ATP
-
stimulation of CDP reduction
ATP
-
stimulation of ADP reduction
ATP
-
stimulation of UDP reduction
ATP
-
stimulation of CDP reduction
ATP
-
ATP is an allosteric effector
ATP
-
activation by ATP has a regulatory function
ATP
-
stimulation of UDP reduction
ATP
-
stimulation of CDP reduction
ATP
-
stimulates the reduction of CDP and ADP
ATP
allosteric effector of CDP reaction
ATP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
ATP
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
ATP
-
stimulation of CDP reduction
ATP
-
reduction of CDP is dependent on ATP or adenyl-5'-yl iminodiphosphate
ATP
-
required for CDP reduction
ATP
-
stimulation of UDP reduction
ATP
-
stimulation of CDP reduction
ATP
-
activation by ATP has a regulatory function
ATP
-
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
ATP
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
ATP
-
stimulation of CDP reduction
ATP
-
reduction of CDP and UDP requires 1-2 mM ATP
ATP
-
further stimulation of dTTP activated GDP reduction
ATP
-
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
ATP
-
activation by ATP has a regulatory function
ATP
Tequatrovirus T4
-
stimulation of UDP reduction
ATP
Tequatrovirus T4
-
stimulation of CDP reduction
ATP
-
stimulation of CDP reduction
ATP
-
most effective activator
dATP
-
activates
dATP
-
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP
stimulation of CDP reduction
dATP
-
stimulation of CDP and UDP reduction
dATP
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
dATP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
dATP
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dATP
-
stimulation of ADP reduction
dATP
-
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
dATP
-
6fold stimulation of GDP reduction
dATP
-
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
dATP
-
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
dATP
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
dATP
-
stimulation of GDP reduction
dATP
-
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
dATP
-
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dATP
-
strong stimulation of CDP reduction
dATP
Tequatrovirus T4
-
stimulation of CDP and UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of CDP and ADP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
-
stimulation of UDP reduction
dCTP
Tequatrovirus T4
-
stimulation of UDP reduction
dCTP
Tequatrovirus T4
-
stimulation of CDP reduction
dCTP
-
stimulation of UDP reduction
dGTP
-
stimulation of ADP reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
stimulation of CDP reduction
dGTP
-
stimulation of GDP reduction
dGTP
-
stimulation of ADP reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
the binding of effector dGTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
dGTP
-
stimulation of ADP reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
stimulates the reduction of CDP and ADP
dGTP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The O6 and protonated N1 of dGTP direct specificity for ADP
dGTP
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The O6 and protonated N1 of dGTP direct specificity for ADP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dGTP
-
required for ADP reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
activation of ADP reduction
dGTP
-
stimulation of ADP reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
required for ADP reduction, maximal activity with 0.01 mM dGTP
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
stimulation of tubercidin diphosphate reduction
dGTP
-
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The O6 and protonated N1 of dGTP direct specificity for ADP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dGTP
-
slight stimulation of CDP reduction
dGTP
Tequatrovirus T4
-
-
dGTP
Tequatrovirus T4
-
stimulation of ADP reduction
dGTP
Tequatrovirus T4
-
stimulation of tubercidin diphosphate reduction
dGTP
Tequintavirus T5
-
-
dGTP
-
stimulation of tubercidin diphosphate reduction
Dithiols
-
required for in vitro reduction
-
Dithiols
-
required for reduction of CDP in vitro
-
dithiothreitol
-
required for optimal activity
dithiothreitol
-
slight activation
dithiothreitol
-
optimal in vitro activity with 10 mM, inhibition above
dithiothreitol
-
high concentrations serve as in vitro hydrogen donor
DTT
-
-
DTT
-
required for activity
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
stimulation of CDP reduction
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
-
stimulation of ADP reduction
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The 5-methyl, O4, and N3 groups of dTTP contributes to specificity for GDP
dTTP
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
required for GDP reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
-
only binds to the specificity site (s-site), is able to stimulate tetramer formation
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of GDP reduction
dTTP
-
absolutely required for GDP reduction, less than 10% activity in the absence of dTTP, maximal stimulation with 0.001-0.1 mM dTTP in the absence of ATP and 0.1-1 mM in the presence of ATP, inhibition above
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
required for ADP reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
-
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dTTP
-
slight stimulation of CDP reduction
dTTP
Tequatrovirus T4
-
stimulation of UDP reduction
dTTP
Tequatrovirus T4
-
stimulation of CDP reduction
dTTP
Tequatrovirus T4
-
stimulation of GDP reduction
dTTP
Tequatrovirus T4
-
stimulation of purine riboside diphosphate reduction
dTTP
Tequatrovirus T4
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
Tequatrovirus T4
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
Tequatrovirus T4
-
stimulation of benzimidazoleriboside diphosphate reduction
dTTP
Tequintavirus T5
-
-
dTTP
-
stimulation of UDP reduction
dTTP
-
stimulation of CDP reduction
dTTP
-
stimulation of purine riboside diphosphate reduction
dTTP
-
stimulation of 2,6-diaminopurine riboside reduction
dTTP
-
stimulation of 2-aminopurineriboside diphosphate reduction
dTTP
-
stimulation of benzimidazoleriboside diphosphate reduction
E. coli thioredoxin reductase
Tequatrovirus T4
-
absolute requirement
-
E. coli thioredoxin reductase
Tequatrovirus T4
-
enzyme induced in Escherichia coli by infection with bacteriophage T4
-
NrdI
involved in binding of FMN. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. Lys260 is involved in a hydrogen bond network with the strictly conserved residues Tyr256 and NrdI Glu110, mechanism of MnII 2-NrdF activation by NrdIhq and O2, overview
-
NrdI
-
is an essential player in Escherichia coli class Ib RNR cluster assembly, overview. Preparation of recombinant N-terminally His6-tagged NrdI
-
phosphate
-
50 mM, slight stimulation, inhibition at 200 mM
phosphate
-
up to 50 mM, pH 6.7: necessary for activity, decrease of activity at higher values
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
quantitative activation
-
additional information
-
the R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview
-
additional information
-
ribonucleoside effectors are exclusively bound at effector binding sites on subunit B1 controlling substrate specificity and activity
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
enzyme activation mechanism and kinetics, overview
-
additional information
mechanism for the activation of peroxy intermediates in binuclear non-heme iron enzymes for reactivity
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
TTP, dATP, TTP/GDP, TTP/ATP, and TTP/dATP, 1. TTP bound at the S-site, 2. dATP bound at the S-site, 3. TTP bound at the S-site and GDP at the C-site, 4. TTP bound at the S-site and ATP at the A-site, and 5. TTP bound at the S-site and dATP at the A-site
-
additional information
-
enzyme of cells first treated with 2,6-dichlorophenolindophenol has a complete dependence on NADPH which can also be met by dithiothreitol or dihydrolipoic acid
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
subunit R1 has 2 effector-binding sites per polypeptide chain: one activity site for dATP and ATP, with dATP-inhibiting and ATP-stimulating catalytic activity and a second specificity site for dATP, ATP, dTTP and dGTP directing substrate specificity
-
additional information
-
overview: nucleoside 5'-diphosphates as effectors of mammalian ribonucleotide reductase
-
additional information
-
comprehensive and quantitative model for allosteric control of mRR enzymatic activity based on molecular mass, ligand binding and enzyme activity studies
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
Tequatrovirus T4
-
overview: stimulation of various enzymes
-
additional information
Tequatrovirus T4
-
stimulation by effector nucleotides
-
additional information
Tequatrovirus T4
-
stimulation with various substrates
-
additional information
-
overview: stimulation of various enzymes
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation by effector nucleotides
-
additional information
-
stimulation with various substrates
-
additional information
-
stimulation with various substrates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterodimer
eukaryotic RNRs comprise alpha2beta2 heterodimers, the large and small subunits show strong interaction
heterotetramer
-
R1R2 complex
hexamer
-
4 * 45000 + 1 * 45000 + 1 * 75000, regenerating liver
homotetramer
4 * 107106, calculated from sequence
monomer
-
beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form
multimer
-
alphanbetan multi-subunit protein complex consisting of subunit types RR1 and RR2, the alpha or RR1 subunit contains the catalytic C site and two allosteric sites, while the beta or RR2 subunit houses a stable tyrosyl free radical that is transferred some 35 A to the catalytic site to initiate radical-based chemistry on the substrate
octamer
-
4 * 107000, subunit NrdA + 4 * 47000, subunit NrdB, SDS-PAGE
trimer
alpha,beta2, 1 * 81200 + 2 * 37900, deduced from nucleotide sequence
?
-
-
?
-
x * 84000 + x * 58000, 84000 Da subunit is predominantly monomeric under experimental conditions, 58000 Da subunit may be oligomeric, SDS-PAGE
?
-
x * 34000, R2F subunit, DSD-PAGE
?
-
x * 34000, R2F subunit, DSD-PAGE
-
?
-
2 * 90000 + x * ?, Novikoff hepatoma cells
?
-
x * 45000 + 1 * 75000 + 1 * 45000, holoenzyme may have an alpha4,beta,beta' structure, SDS-PAGE
?
-
2 * 90000 + x * 75000, most likely 1 75000 Da subunit, SDS-PAGE
dimer
-
alphabeta, class Ib RNR is composed of two subunits alpha (NrdE) and beta (NrdF). Beta contains the metallo-cofactor, essential for the initiation of the reduction process
dimer
-
alphabeta, class Ib RNR is composed of two subunits alpha (NrdE) and beta (NrdF). Beta contains the metallo-cofactor, essential for the initiation of the reduction process
-
dimer
Herpes simplex virus
-
1 * 136000 + 1 * 38000, molecular weight for subunit 1 deduced from sequence: 124017 Da, difference may be due to phosphorylation, SDS-PAGE
dimer
-
alpha,beta, 1 * 100000 + 1 * 100000, Molt F4 lymphoblast cells
dimer
-
2 * 60200, dimer appears to dissociate in the absence of Ca2+ into monomers, SDS-PAGE
dimer
-
beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form
monomer or dimer
-
alpha or alpha2, class II RNRs
monomer or dimer
-
class II enzymes show a monomeric or dimeric structure
monomer or dimer
-
alpha or alpha2, class II RNRs
monomer or dimer
-
alpha or alpha2, class II RNRs
monomer or dimer
-
class II enzymes show a monomeric or dimeric structure
monomer or dimer
-
class II enzymes show a monomeric or dimeric structure
oligomer
-
class I enzymes show a alpha2beta2 complex structure, modeling
oligomer
-
RNRs are composed of alpha- and beta-subunits that form active (alpha)n(beta)m, with n or m being 2 or 6, complexes. Subunit alpha binds NDP substrates, i.e. CDP, UDP, ADP, and GDP, C site, as well as ATP and dNTPs, i.e. dATP, dGTP, TTP, allosteric effectors that control enzyme activity (A site) and substrate specificity, S site
oligomer
-
class I enzyme show a alpha2beta2 complex structure, modeling
oligomer
-
class I enzyme show a alpha2beta2 complex structure, modeling
tetramer
-
2 * 84000 + 2 * 55000, SDS-PAGE
tetramer
-
2 * R1 subunit + 2 * R2 subunit
tetramer
-
alpha2beta2, with subunits alpha1, alpha2, beta1, and beta2
tetramer
-
alpha2,beta2, 160000 Da subunit B1 and 78000 Da subunit B2, each consisting of 2 identical or similar proteins
tetramer
-
alpha,alpha'beta2, 2 * 82000 + 2 * 78000, each subunit composed of 2 polypeptide chains, subunit B1, 82000 Da, sedimentation equilibrium centrifugation, subunit B2, low speed sedimentation equilibrium centrifugation
tetramer
-
alpha, alpha',beta2, 2 * 80000 + 2 * 39000, SDS-PAGE
tetramer
-
alpha2beta2 complex
tetramer
-
2 * subunit R1 + 2 * subunit R2
tetramer
-
alpha2beta2, class I RNRs
tetramer
-
class I RNR is a tetramer formed by two homodimers, subunit R1 encoded by the nrdA gene and subunit R2 encoded by the nrdB gene
tetramer
-
class Ib RNR is composed of two homodimeric subunits: alpha2 or NrdE, where nucleotide reduction occurs, and beta2 or NrdF, which contains an unidentified metallocofactor that initiates nucleotide reduction
tetramer
-
class I RNR is a tetramer formed by two homodimers, subunit R1 encoded by the nrdA gene and subunit R2 encoded by the nrdB gene
-
tetramer
-
alpha2,beta2, 160000 Da subunit B1 and 78000 Da subunit B2, each consisting of 2 identical or similar proteins
-
tetramer
-
2 * 160000, subunit R1, + 2 * 78000, subunit R2, the catalytic active enzyme forms a dimer of homodimers
tetramer
-
2 * M1-subunit + 2 * M2-subunit
tetramer
-
RNR is a tetramer consisting of two non-identical homodimers. The two identical M2 subunits regulate the substrate specificity of the enzyme, while the other two identical M1 subunits are responsible for the activity by binding the ribonucleotides and allosteric effectors
tetramer
-
1:1 complex of two homodimeric subunits, hRRM1 and hRRM2
tetramer
-
the enzyme consists of M1, M2, and p53R2 subunits in an alphabeta2gamma constellation
tetramer
-
alpha2beta2, class I RNRs
tetramer
-
4 * 37 442.98, subunit R2, mass spectrometry, 4 * 31000, recombinant subunit R2, SDS-PAGE
tetramer
-
alpha2beta2, class I RNRs
tetramer
-
alpha2beta2, class I RNRs
tetramer
-
alpha2,betabeta, 2 * 96900 (PFR1) + 1 * 40600 (PFR2) + 1 * 39000 (PFR4), SDS-PAGE
tetramer
-
beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form
tetramer
the enzyme activity requires formation of a complex between subunits R1 and R2 in which the R2 C-terminal peptide binds to R1
tetramer
-
alpha2beta2, class I RNRs
tetramer
-
alpha2,beta2, 2 * 70000 + 2 * 36000, SDS-PAGE
tetramer
Tequatrovirus T4
-
alpha2beta2, 2 * 85000 + 2 * 35000, enzyme induced in Escherichia coli after infection with bacteriophage T4, SDS-PAGE
tetramer
Tequatrovirus T4
-
alpha2beta2, 2 * 84000 + 2 * 43500, SDS-PAGE
additional information
-
at physiological concentrations, alpha-subunit NrdE is a monomer and beta-subunit NrdF in complex with dimanganic-tyrosyl radical cofactor is a dimer. A 1:1 mixture of NrdE:NrdF, however, is composed of a complex mixture of structures
additional information
-
at physiological concentrations, alpha-subunit NrdE is a monomer and beta-subunit NrdF in complex with dimanganic-tyrosyl radical cofactor is a dimer. A 1:1 mixture of NrdE:NrdF, however, is composed of a complex mixture of structures
-
additional information
interaction of the alpha2 and beta2 subunits during the reaction, comparison to the RNR from Escherichia coli, overview
additional information
-
interaction of the alpha2 and beta2 subunits during the reaction, comparison to the RNR from Escherichia coli, overview
additional information
-
hybrid holoenzyme, consisting of the small manganese-containing R2F subunit and the large catalytic subunit R1E
additional information
-
hybrid holoenzyme, consisting of the small manganese-containing R2F subunit and the large catalytic subunit R1E
-
additional information
-
tyrosyl radical is stabilized by an iron center
additional information
proposed in vitro mechanism for the assembly of the diferric tyrosyl radical cofactor of subunit R2
additional information
-
the active form of B2 subunit contains a tyrosyl radical essential for activity
additional information
-
the active form of B2 subunit contains a tyrosyl radical essential for activity
additional information
-
each catalytic turnover by aerobic ribonucleotide reductase requires the assembly of the two proteins, R1 (alpha2) and R2 (beta2), to produce deoxyribonucleotides for DNA synthesis
additional information
-
2 * R1 subunit + 2 * R2 subunit, cross-talk Between the C-terminus of one subunit R1 monomer and the active site of its neighboring monomer, overview
additional information
interaction of the alpha2 and beta2 subunits during the reaction, comparison to the RNR from Chlamydia trachomatis, overview
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
-
subunit R1 contains the substrate binding site and catalyzes dehydroxylation of the 2'-hydroxyl group of the ribose ring. The tyrosine radical in R2 is in the neutral deprotonated form with the oxidized Fe(III)Fe(III) active site
additional information
a complex between alpha2 and beta2 subunits forms an unprecedented alpha4beta4 ring-like structure in the presence of the negative activity effector dATP, while the active conformation is alpha2beta2. Under physiological conditions, the enzyme exists as a mixture of transient alpha2beta2 and alpha4beta4 species whose distributions are modulated by allosteric effectors. This interconversion between entails dramatic subunit rearrangements
additional information
ribonucleoside-diphosphate reductase subunit M2 B may substitute for small enzyme subunit hRRM2 to form a functional holoenzyme with large subunit hRRM1. The holoenzyme with subunit M2 B can only achieve 40-75% kinetic activity of that with hRRM2. Both small subunits share the same binding site on large subunit hRRM1. The effectors ATP or dATP can regulate holoenzyme activity independent of the small subunit
additional information
-
one monomer can swivel between two conformations and impose significant influences on helix D and helix B of the opposite monomer. This change ultimately affects the orientation of D100 and, thus, the integrity of the binuclear iron environment. Structural basis of B helix disorder and the N-terminal swivel region, overview
additional information
-
dATP-induced oligomerization, overview, modeling of the holo-complex
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
in hypoxic conditions the small subunit of the ribonucleotide reductase enzyme is switched from RRM2 to RRM2B in order to facilitate nucleotide production and ongoing replication. Specific residues within RRM2B are identified that are responsible for maintaining activity in hypoxia
additional information
-
class I RNRs are composed of a heterotetramer, which is in turn composed of two homodimers of the R1 and R2 subunits. The R1 subunit contains the active site as well as the sites for allosteric regulation
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
-
nucleotide binding to the specificity site drives formation of an active R1,2R2,2 dimer, ATP or dATP binding to the adenine-specific site results in formation of an inactive tetramer and ATP binding to the hexamerization site drives formation of an active R1,6R2,6 hexamer which is probably the major active form in mammalian cells
additional information
-
enzyme in Ehrlich ascites tumor cells consits of two nonidentical subunits: an effector-binding subunit, EB, and a non-heme iron containing subunit, NHI, since their relative levels are not coordinately regulated the stoichiometry of the whole enzyme varies with the cell cycle
additional information
-
composition of the enzyme is not constant, but is altered in presence of effectors
additional information
-
large subunit R1 contains binding sites for substrates and allosteric effectors, smaller subunit R2 contains non-heme iron and a tyrosyl free-radical
additional information
-
large subunit R1 contains binding sites for substrates and allosteric effectors, smaller subunit R2 contains non-heme iron and a tyrosyl free-radical
additional information
-
in presence of dTTP, subunit R1 forms dimers. In presence of dATP or ATP, subunit R1 forms hexamers of 544000 Da, which interact with the subunit R2 dimer to form an enzymatically active protein complex alpha6beta2. The complex can be in activated or inhibited state depending on whether ATP or dATP is bound. Complex alpha6beta2 is the major form of enzyme at physiological levels of subunits and nucleotides
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
the active class Ib ribonucleotide reductase can use two different small, cofactor-housing subunits, R2F-1 and R2F-2, with similar activity
additional information
-
enzyme is a complex of the NrdA protein harboring the active site and the allosteric sites and the NrdB protein harboring a tyrosyl radical. Wild-type enzyme consists of four NrdA and four NrdB subunits. A truncated NrdA lacking the N-terminal ATP-cone forms an NrdA2NrdB2 complex
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
-
88000-90000 Da M1 subunits are degraded into 40000 Da fragments in proliferately quiescent liver cells, intact subunits are only accumulated when the cells replicate DNA
additional information
-
subunits Y1 and Y2 constitute the active enzyme, large subunit Y3 has no activity, subunit Y4 may function as a chaperone
additional information
-
C-terminal domain of subunit R1 acts in trans to reduce the active site of its neighbouring monomer and interacts with the N-terminal domain of neighbouring R1. Inhibitor protein Sml1 competes with the C-terminal domain of R1 for association with the N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle
additional information
-
enzyme consists of two homodimeric subunits, R1 and R2. In Saccharomyces cerevisiae, there are two R2 subunits named beta and beta, the active form in the holoenzyme being a dimer betabeta. Isoform beta plays a crucial role in cluster assembly
additional information
-
under normal conditions, the cell assembles stoichiometric amounts of tyrosyl radicals per betabeta subunit dimer and modulation of tyrosyl radical concentration is not involved in regulation of enzyme activity
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
-
catalytic subunit U2 contains a tyrosyl radical essential for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
morme
AtRNR2B induction is abolished in the rad9-rad17 double mutant, transgenic plant phenotypes, overview
F127Y
-
similar CDP reductase activity as wild-type
F127Y/Y129F
-
10-15% of wild-type CDP reductase activity
W51F
-
site-directed mutagenesis, the decay of the Mn(IV)/Fe(IV) intermediate is slightly affected
Y129F
-
no CDP reductase activity
Y222F
-
the substitution by site-directed mutagenesis retards the intrinsic decay of the Mn(IV)/Fe(IV) intermediate by about 10fold and diminishes the ability of ascorbate to accelerate the decay by about 65fold but has no detectable effect on the catalytic activity of the Mn(IV)/Fe(III)-R2 product
Y338F
-
site-directed mutagenesis, substitution of Y338, the cognate of the subunit interfacial R2 residue in the R1 S R2 PCET pathway of the conventional class I RNRs, has almost no effect on decay of the Mn(IV)/Fe(IV) intermediate but abolishes catalytic activity
G392S
-
temperature-sensitive protein with complete splicing activity at 17 and 28°C but not at 37°C or higher
G392S/C539G
-
the cleavage at the ribonucleotide reductase RIR1 intein C-terminus is blocked, but other cleavage activities can be efficiently performed at 17°C. The mutant variant possesses the properties of low-temperature-induced cleavage at the intein N-terminus
C225A
-
4-6% of wild-type activity
C439A
-
4-6% of wild-type activity
C439S
-
the C439S mutant of the Escherichia coli R1 is catalytically inactive in vitro
C462S
-
in the presence of dithiothreitol the major product formed by interaction with CDP is cytosine
C754A
-
active with dithiothreitol as reductant, 3% of wild type activity with thioredoxin
C759A
-
active with dithiothreitol as reductant, 3% of wild type activity with thioredoxin
C759S
-
C759 may play a role in the relay of electrons between thioredoxin and subunit B1
D84E
the mutation provides a ligand environment similar to that found in methane monooxygenase, MMO, renders this residue bidentate, and Glu204 becomes monodentate. The RNR mutant, however, remains distinct from MMO, which has a beta-1,1 type Glu-bridge, most likely due to the effects of second sphere residues
N238A
-
the monomeric R1 protein is able to dimerize when bound by both substrate and effector and is able to reduce ribonucleotides with a comparatively high capacity
W48A/Y122F
the reaction remains at the level of the peroxo-intermediate, structural analysis
W48F/D84E
the reaction remains at the level of the peroxo-intermediate, structural analysis
Y122H
the specific activity of mutant enzyme preparation is less than 0.5% of the wild-type activity. Mutant of R2 protein subunit, the mutant contains a novel stable paramagnetic center, named H. Deteiled characterization of center H, using 1H2H-14N/15N- and 57Fe-EDDOR in comparison with the FeIIIFeIV intermediate X observed in the iron reconstitution reaction of R2, a new tyrosyl radical on Phe208 as ligand to the diiron center
Y730F
-
site-directed mutagenesis, the mutant excludes a direct superexchange mechanism between C439 and Y731 in radical transport, overview
D16R
-
site-directed mutagenesis, the mutant retains 55% of wild-type activity for CDP reduction, and 67% for ADP reduction, it is not inhibited and does not form hexamers at physiologically relevant dATP concentrations
H2E
-
site-directed mutagenesis, the mutant retains 56% of wild-type activity for CDP reduction, and 56% for ADP reduction
K95E
mutation in small subunit M2, results in dimer disassembly and enzyme activity inhibition. Mutant is capable of generating the diiron and tyrosyl radical cofactor, but the disassembly of the M2 dimer reduces its interaction with the large subunit M1. The transfection of the wild-type M2 but not the K95E mutant rescues theG1/S phase cell cycle arrest and cell growth inhibition caused by the siRNA knockdown of M2
K95E/E98K
charge-exchanging double mutation, recovers the dimerization and activity lost in mutant K95E
R265A
-
mutant in subunit R2, about 10% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type
R265E
-
mutant in subunit R2, about 40% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type
R265Q
-
mutant in subunit R2, about 1% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type
R265Y
-
mutant in subunit R2, about 4% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type
Y177F
-
tyrosyl residue involved in radical formation
Y370F
-
mutation in R2 subunit, no activity
Y370W
-
mutation in R2 subunit, point mutation does not affect the ability to form a normal diferric iron/tyrosyl radical center, 1.7% of wild-type activity probably due to slow radical transfer
E106A/E126A
mutant enzyme completely loses the ability to be inhibited by dATP. Like the wild-type protein the mutant enzyme can bind approximately three dATP per polypeptide. The mutant enzyme loses the ability to tetramerize and only forms dimers regardless of allosteric effector
H72A/D73A/Y830A
the mutant enzyme forms inactive tetramers in the presence of any allosteric effector, the mutant enzyme partially loses its propensity to be inhibited by dATP. Like the wild-type protein the mutant enzyme can bind approximately three dATP per polypeptide
R119D
mutant enzyme completely loses the ability to be inhibited by dATP. Like the wild-type protein the mutant enzyme can bind approximately three dATP per polypeptide. The mutant enzyme loses the ability to tetramerize and only forms dimers regardless of allosteric effector
C428S
-
mutantion is lethal. Cells carrying both the C428S and the SX2S mutation of CX2C motif on plasmids are viable and form colonies with an efficiency similar to that of the wild-type control showing interallelic complementation
K387N
-
affords higher activity due to increased tyrosyl radical content
Q288A
mutation causes severe S phase defects in cells that use the enzyme as the sole source of of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, Q288A mutants show 15% of ADP reduction, whereas they show 23% of CDP reduction. There is a 6fold loss of affinity for ADP binding and a 2fold loss of affinity for CDP. Q288A can support mitotic growth, albeit with a severe S phase defect
R293A
mutation causes lethality in cells that use the enzyme as the sole source of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, R293A mutants show 4% of ADP reduction, whereas they show 20% CDP reduction. The mutant is unable to bind ADP and binds CDP with 2fold lower affinity compared to wild-type. X-ray structures of R293A complexed with dGTP and AMPPNP reveal that ADP is not bound at the catalytic site, and CDP binds farther from the catalytic site compared to wild type. R293A cannot support mitotic growth
C225S
-
C225 appears to be one of the participants in the direct reduction of substrate
C225S
-
major product formed by interaction with CDP is cytosine
Y122F
mutant enzyme cannot generate a Y122 tyrosyl radical necessary for catalysis, 0.5% of wild-type activity
Y122F
-
subunit R2, study on kinetics of decay of W48 cation radical
Y122F/Y356F
0.5% of wild-type activity
Y122F/Y356F
-
subunit R2, study on kinetics of decay of W48 cation radical
Y356F
similar properties as wild-type
Y356F
-
subunit R2, study on kinetics of decay of W48 cation radical
D287A
the mutant enzyme (mutation in the ribonucleoside-diphosphate reductase large subunit RRM1) is deficient in allosteric regulation by dGTP and dTTP, but not ATP/dATP
D287A
the mutant enzyme is deficient in allosteric regulation by dGTP and dTTP, but not ATP/dATP
D57N
-
site-directed mutagenesis, binding kinetics to clofarabine di- and triphosphate inhibitors compared to the wild-type enzyme, overview
D57N
-
site-directed mutagenesis, the mutant is not inhibited and does not form hexamers at physiologically relevant dATP concentrations, the mutation of Asp 57 to Asn abolishes the salt-bridge and change the electrostatic environment of the A-site, resulting in loss of allosteric regulation by dATP
D57N
-
mutation in R1 subunit, in contrast to wild-type dATP stimulates CDP reduction, GDP reduction is inhibited by dGTP, ADP reduction is inhibited by dTTP similar to wild-type, this suggests that the mutant enzyme binds both ATP and dATP to the activity site but does not distinguish between them when it comes to catalysis
D57N
-
mutant of the catalytic subunit mR1 is not inhibited by dATP because of a block in the formation of R1(4b)
additional information
atTSO2 transcription is only activated in response to double-strand breaks dependent upon AtE2Fa. ATso2 mutant is hypersensitive to bleomycin, transgenic plant phenotypes, overview
additional information
atTSO2 transcription is only activated in response to double-strand breaks dependent upon AtE2Fa. ATso2 mutant is hypersensitive to bleomycin, transgenic plant phenotypes, overview
additional information
atTSO2 transcription is only activated in response to double-strand breaks dependent upon AtE2Fa. ATso2 mutant is hypersensitive to bleomycin, transgenic plant phenotypes, overview
additional information
early AtRNR2A induction is decreased in an atr mutant, rnr2a mutants are hypersensitive to hydroxyurea, transgenic plant phenotypes, overview
additional information
early AtRNR2A induction is decreased in an atr mutant, rnr2a mutants are hypersensitive to hydroxyurea, transgenic plant phenotypes, overview
additional information
early AtRNR2A induction is decreased in an atr mutant, rnr2a mutants are hypersensitive to hydroxyurea, transgenic plant phenotypes, overview
additional information
-
construction of truncated R1 mutant DELTA1-248
additional information
Cinqassovirus aeh1
-
insertion of homing endonuclease gene mobE into the nrdA gene coding for the large subunit of ribonucleotide-diphosphate reductase. The insertion splits nrdA into two independent genes but does not inactivate NrdA function. The reconstituted complex of NrdA-a, NrdA-b and sunbunit NrdB has enzymic activity
additional information
-
mutations of resiude C539, the N-terminal residue of the C-extein in the ribonucleotide reductase RIR1 protein, lead to changes of pattern and level of protein-splicing activities
additional information
-
site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit and trapping the 3,4-dihydroxyphenylalanine radical intermediate in the presence of alpha2 subunit dimer, substrate and effector ATP or TTP. 3,4-Dihydroxyphenylalanine radical formation shows fast and slow phases, rapid phases are substrate-mediated conformational changes that place about 50% of the alpha2beta2 complex into an active conformation for turnover. Substrate plays a major role in conformational gating
additional information
-
expression of subunit R2 siRNA 1284, targeting the AA(N19) sequence motif, inhibits R2 expression and active enzyme complex formation in different cell lines, it also inhibits cell growth and proloferation in vitro by blocking in the S-phase of the cell cycle, overview
additional information
-
transfection of RRM2 protein-expressing Hep-G2 cells with constructed potent siRNA, NM_009104, inhibitors of ribonucleotide reductase subunit RRM2 reduce cell proliferation in vitro and in vivo, overview
additional information
construction of transgenic plants using Agrobacterium tumefaciens-mediated transformation. Complementation by gene construct introduction into calli generated from the mature embryos of v3 and st1 mutant kernels, respectively. The stripe1 mutant in Oryza sativa produces chlorotic leaves in a growth stage-dependent manner under field conditions. It is a temperature-conditional mutants that produces bleached leaves at a constant 20°C or 30°C, but almost green leaves under diurnal 30°C/20°C conditions, phenotype, overview. Expression profiles of genes associated with chloroplast development in mutant plants
additional information
construction of transgenic plants using Agrobacterium tumefaciens-mediated transformation. Complementation by gene construct introduction into calli generated from the mature embryos of v3 and st1 mutant kernels, respectively. The stripe1 mutant in Oryza sativa produces chlorotic leaves in a growth stage-dependent manner under field conditions. It is a temperature-conditional mutants that produces bleached leaves at a constant 20°C or 30°C, but almost green leaves under diurnal 30°C/20°C conditions, phenotype, overview. Expression profiles of genes associated with chloroplast development in mutant plants
additional information
construction of transgenic plants using Agrobacterium tumefaciens-mediated transformation. Complementation by gene construct introduction into calli generated from the mature embryos of v3 mutant kernels, respectively. The virescent3 mutant in Oryza sativa produces chlorotic leaves in a growth stage-dependent manner under field conditions. It is a temperature-conditional mutant that produces bleached leaves at a constant 20°C or 30°C, but almost green leaves under diurnal 30°C/20°C conditions, phenotype, overview. Expression profiles of genes associated with chloroplast development in mutant plants
additional information
construction of transgenic plants using Agrobacterium tumefaciens-mediated transformation. Complementation by gene construct introduction into calli generated from the mature embryos of v3 mutant kernels, respectively. The virescent3 mutant in Oryza sativa produces chlorotic leaves in a growth stage-dependent manner under field conditions. It is a temperature-conditional mutant that produces bleached leaves at a constant 20°C or 30°C, but almost green leaves under diurnal 30°C/20°C conditions, phenotype, overview. Expression profiles of genes associated with chloroplast development in mutant plants
additional information
-
truncated NrdA lacking the N-terminal ATP-cone forms an NrdA2NrdB2 complex. Mutant protein is completely resistant to high concentrations of dATP
additional information
-
deletion of C-terminal domain of subunit R1 is lethal. Mutation of CX2C motif to SX2S results in viable, but slowly growing cells. Mutant cells exhibit a prolonged S phase
additional information
construction of heterochimeric enzymes as heterocomplexes containing mammalian R2 C-terminal heptapeptide P7, Ac-1FTLDADF7, and its peptidomimetic P6, 1Fmoc(Me)PhgLDChaDF7, bound to Saccharomyces cerevisiae R1, ScR1, overview
additional information
-
construction of heterochimeric enzymes as heterocomplexes containing mammalian R2 C-terminal heptapeptide P7, Ac-1FTLDADF7, and its peptidomimetic P6, 1Fmoc(Me)PhgLDChaDF7, bound to Saccharomyces cerevisiae R1, ScR1, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.