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.
4-bromo-thiophene-2-carbonyl-S-CoA + amikacin
?
-
-
-
-
?
4-bromo-thiophene-2-carbonyl-S-CoA + gentamicin
?
-
-
-
-
?
4-bromo-thiophene-2-carbonyl-S-CoA + neomycin B
?
-
-
-
-
?
4-bromo-thiophene-2-carbonyl-S-CoA + paromomycin
?
-
-
-
-
?
4-bromo-thiophene-2-carbonyl-S-CoA + tobramycin
?
-
-
-
-
?
5-bromo-thiophene-2-carbonyl-S-CoA + kanamycin A
?
-
-
-
-
?
5-bromo-thiophene-2-carbonyl-S-CoA + neomycin B
?
-
-
-
-
?
6-fluoropicolinyl-CoA + neomycin B
?
-
-
-
-
?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
acetyl-CoA + amikacin
CoA + N3'-acetyl-amikacin
-
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
acetyl-CoA + aminoglycoside-aminocyclitol
CoA + ?
-
-
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
acetyl-CoA + butirosin
CoA + N3'-acetylbutirosin
-
-
-
?
acetyl-CoA + dactimicin
CoA + N4-acetyldactamicin + N4,N6'-diacetyldactimicin
-
the percentage of dactimicin affinity relative to gentamicin C1a is very high (74.6%) only with AAC(3)-I, to the most other enzymes tested, in spite of the bifunctional AAC(6')/APH(2''), dactamicin is stable
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
acetyl-CoA + fortimicin
CoA + N3-acetylfortimicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetyl-gentamicin
-
-
-
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
acetyl-CoA + gentamicin A
CoA + N3'-acetylgentamicin A
-
acetylation at 6% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C
CoA + N3'-acetylgentamicin C
-
acetylation at 86% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
acetyl-CoA + gentamicin C1A
CoA + N3-acetylgentamicin C1A
-
-
-
?
acetyl-CoA + gentamicin C2
CoA + N3'-acetylgentamicin C2
acetyl-CoA + isepamycin
CoA + N3'-acetylisepamycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
acetyl-CoA + lividomycin A
CoA + ?
-
-
-
-
?
acetyl-CoA + neomycin
CoA + ?
-
-
-
?
acetyl-CoA + neomycin
CoA + N2'-acetylneomycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + neomycin
CoA + N3-acetylneomycin
-
-
-
?
acetyl-CoA + neomycin B
CoA + ?
acetyl-CoA + neomycin B
CoA + N3-acetyl-neomycin B
acetyl-CoA + neomycin B
CoA + N3-acetylneomycin B
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
acetyl-CoA + paromomycin
CoA + N3'-acetyl-paromomycin
acetyl-CoA + paromomycin
CoA + N3'-acetylparomomycin
-
-
-
?
acetyl-CoA + paromomycin
CoA + N3-acetylparamomycin
-
-
-
?
acetyl-CoA + ribostamycin
CoA + ?
acetyl-CoA + ribostamycin
CoA + N3-acetylribostamycin
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetyl-sisomicin
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
acetyl-CoA + sisomicin
CoA + N3-acetylsisomicin
-
-
-
?
acetyl-CoA + sisomycin
CoA + N3'-acetylsisomycin
acetyl-CoA + spectinomycin
CoA + N3'-acetylspectinomycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + streptomycin
CoA + ?
wild-type and recombinant enzyme
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyl-tobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
acetyl-CoA + tobramycin
CoA + N3-acetyltobramycin
-
-
-
?
butyryl-CoA + kanamycin A
CoA + N3'-butyryl-kanamycin A
-
-
-
-
?
butyryl-CoA + ribostamycin
CoA + ?
-
-
-
?
desulfo-CoA + ribostamycin
?
-
-
-
?
glutaryl-CoA + kanamycin A
?
-
-
-
-
?
glycyl-CoA + amikacin
CoA + N3'-glycyl-amikacin
-
-
-
-
?
glycyl-CoA + gentamicin
CoA + N3'-glycyl-gentamicin
-
-
-
-
?
glycyl-CoA + kanamycin A
CoA + N3'-glycyl-kanamycin A
-
-
-
-
?
glycyl-CoA + neomycin B
CoA + N3-glycylneomycin B
-
-
-
-
?
glycyl-CoA + sisomicin
CoA + N3'-glycyl-sisomicin
-
-
-
-
?
malonyl-CoA + amikacin
CoA + N3'-malonyl-amikacin
-
-
-
-
?
malonyl-CoA + gentamicin
CoA + N3'-malonyl-gentamicin
-
-
-
-
?
malonyl-CoA + kanamycin A
CoA + N3'-malonylkanamycin A
-
-
-
-
?
malonyl-CoA + neomycin B
CoA + N3-malonylneomycin B
-
-
-
-
?
malonyl-CoA + ribostamycin
CoA + ?
-
-
-
?
methylmalonyl-CoA + neomycin B
CoA + N3-methylmalonylneomycin B
-
-
-
-
?
N-propionyl-CoA + amikacin
CoA + N3'-propionyl-amikacin
-
-
-
-
?
N-propionyl-CoA + gentamicin
CoA + N3'-propionyl-gentamicin
-
-
-
-
?
n-propionyl-CoA + kanamycin A
CoA + N3'-n-propionylkanamycin A
-
-
-
-
?
N-propionyl-CoA + kanamycin A
CoA + N3'-propionyl-kanamycin A
-
-
-
-
?
N-propionyl-CoA + neomycin B
CoA + N3-propionylneomycin B
-
-
-
-
?
N-propionyl-CoA + paromomycin
CoA + N3'-propionyl-paromomycin
-
-
-
-
?
N-propionyl-CoA + sisomicin
CoA + N3'-propionyl-sisomicin
-
-
-
-
?
N-propionyl-CoA + tobramycin
CoA + N3'-propionyl-tobramycin
-
-
-
-
?
propionyl-CoA + ribostamycin
CoA + ?
-
-
-
?
additional information
?
-
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + a 2-deoxystreptamine antibiotic
CoA + N3-acetyl-2-deoxystreptamine antibiotic
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
-
-
-
?
acetyl-CoA + amikacin
CoA + N3'-acetylamikacin
wild-type and recombinant enzyme
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
Arizona sp.
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
-
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
-
-
?
acetyl-CoA + apramycin
CoA + N3'-acetylapramycin
-
a wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3''-acetyldibekacin
-
acetylation at 8% the rate of gentamicin C1
-
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
product identification by high-field NMR
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
-
-
?
acetyl-CoA + dibekacin
CoA + N3-acetyldibekacin
-
product identification by high-field NMR
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + gentamicin
CoA + N3'-acetylgentamicin
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
best substrate
-
-
?
acetyl-CoA + gentamicin C1
CoA + N3'-acetylgentamicin C1
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N3'-acetylgentamicin C1a
-
acetylation at 60% the rate of gentamicin C1
-
?
acetyl-CoA + gentamicin C2
CoA + N3'-acetylgentamicin C2
-
-
-
-
?
acetyl-CoA + gentamicin C2
CoA + N3'-acetylgentamicin C2
-
acetylation at 84% the rate of gentamicin C1
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + kanamycin
CoA + N3'-acetylkanamycin
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
acetylation at 7% the rate of gentamicin C1
-
-
?
acetyl-CoA + kanamycin A
CoA + N3'-acetylkanamycin A
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3'-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
acetyl-CoA + kanamycin B
CoA + N3-acetylkanamycin B
-
-
-
?
acetyl-CoA + neomycin B
CoA + ?
-
-
-
-
?
acetyl-CoA + neomycin B
CoA + ?
-
-
-
-
?
acetyl-CoA + neomycin B
CoA + N3-acetyl-neomycin B
-
-
-
-
?
acetyl-CoA + neomycin B
CoA + N3-acetyl-neomycin B
-
-
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
-
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
-
the much higher treshold value for the modification of netilmicin as compared with the one for the modification of sisomicin is due to the 1-N side chain
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
-
the much higher treshold value for the modification of netilmicin as compared with the one for the modification of sisomicin is due to the 1-N side chain
-
-
?
acetyl-CoA + netilmicin
CoA + N3'-acetylnetilmicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + paromomycin
CoA + N3'-acetyl-paromomycin
-
-
-
-
?
acetyl-CoA + paromomycin
CoA + N3'-acetyl-paromomycin
-
-
-
-
?
acetyl-CoA + ribostamycin
CoA + ?
-
-
-
?
acetyl-CoA + ribostamycin
CoA + ?
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetyl-sisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetyl-sisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
-
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
wild-type and recombinant enzyme
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
acetylation at 51% the rate of gentamicin C1
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
best substrate
-
?
acetyl-CoA + sisomycin
CoA + N3'-acetylsisomycin
-
-
-
?
acetyl-CoA + sisomycin
CoA + N3'-acetylsisomycin
-
-
-
-
?
acetyl-CoA + sisomycin
CoA + N3'-acetylsisomycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
wild-type and recombinant enzyme
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
acetylation at 6% the rate of gentamicin C1
-
-
?
acetyl-CoA + tobramycin
CoA + N3'-acetyltobramycin
-
-
-
-
?
additional information
?
-
determination of imipenem, meropenem, and gentamicin resistant clinical isolates
-
-
?
additional information
?
-
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
?
additional information
?
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
?
additional information
?
-
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
?
additional information
?
-
the enzyme shows a unique profile of the reaction. No activity with kanamycin A, amikacin, netilmicin, neomycin B, and apramycin
-
-
?
additional information
?
-
-
binding of aminoglycosides to AAC-VIa is enthalpically favored and entropically disfavored with a net result of favorable Gibbs energy. A net deprotonation of the enzyme, ligand, or both accompanies the formation of binary and ternary complexes. Poor substrates: kanamycn A, ribostamycin, neomycin B
-
-
-
additional information
?
-
-
no substrates are amikacin
-
-
?
additional information
?
-
-
no activity with benzoyl-CoA, acetoacetyl-CoA, crotonyl-CoA, isovaleryl-CoA, palmitoyl-CoA, and DL-3-hydroxy-butyryl-CoA by AAC(6')-APH(2'')
-
-
?
additional information
?
-
-
no substrates are amikacin
-
-
?
additional information
?
-
-
no substrates are amikacin
-
-
?
additional information
?
-
-
no substrates are amikacin
-
-
?
additional information
?
-
-
lividomycin A, butirosin A and B
-
-
?
additional information
?
-
-
CoASH associates with a high-affinity, catalytic site and with a secondary, low-affinity site that overlaps with the antibiotic binding pocket. The binding of CoASH to the high-affinity site occurs with a small, unfavorable enthalpy and a favorable entropy. Binding to the second site is highly exothermic and is accompanied by an unfavorable entropic contribution. The presence of an aminoglycoside alters the binding of CoASH to the enzyme dramatically such that the binding occurs with a favorable enthalpy and an unfavorable entropy. This is irrespective of which aminoglycoside is the cosubstrate and occurs without a significant change in the affinity of CoASH for the enzyme. The presence of antibiotics eliminates binding of CoASH to the second site
-
-
?
additional information
?
-
-
enzyme displays molecular size-dependent stoichiometry where binding stoichiometries are 1.5-2.0 for small antibiotics and 1.0 for larger. Antibiotic-enzyme interaction occurs with a favorable enthalpy and a compensating unfavorable entropy. The presence of coenzyme A significantly increases the affinity of the antibioticthe enthalpy of binding becomes more favored by 1.7-10.0fold in the presence of the cosubstrate CoASH, while the entropy becomes 2.0-22.5fold less favored. The overall free energy change is still only 1.0-1.9 kcal/mol from binary to ternary for all antibiotics tested, similar to those for other aminoglycoside-modifying enzymes
-
-
?
additional information
?
-
isoform AAC-IIIb demonstrates fast antibiotic turnover rates, high antibiotic affinity. Aminoglycoside binding becomes more enthalpically favored and entropically disfavored when CoASH is complexed to AAC-IIIb. The enzyme catalytically and enthalpically favor those aminoglycosides with amine groups at the 2' carbon and show an increase in affinity of all aminoglycosides when CoASH is present
-
-
?
additional information
?
-
-
no substrates are amikacin
-
-
?
additional information
?
-
-
AAC(3)-Id is responsible for the gain of resistance to diverse agents, i.e. gentamicin C1a, gentamicin C1, sisomicin, neomycin, dibekacin, kanamycin, tobramycin, amikacin, netilmicin, apramycin, dactimicin, spectinomycin, streptomycin, lividomycin, and butirosin, in Salmonella enterica serovar Haifa, 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.
0.00067
apramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.237
butirosin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
1.16
butyryl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0029 - 0.0189
gentamicin
0.002 - 0.066
gentamicin C1
0.00012
gentamicin C1a
-
-
0.003
gentamicin C2
-
pH 7.6, 25°C
0.00097
gentamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.002 - 0.238
kanamycin A
0.0026 - 0.0802
kanamycin B
0.0036
lividomycin A
-
pH 7.6, 25°C
0.234 - 0.477
malonyl-CoA
0.0886
n-propionyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
0.00036
neomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0012 - 0.0148
neomycin B
0.042
netilmicin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00015 - 0.0033
paromomycin
0.499
propionyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0023 - 0.0031
ribostamycin
0.00057 - 0.015
sisomicin
0.00033 - 0.0015
sisomycin
0.0013 - 0.106
tobramycin
additional information
additional information
-
0.0013
acetyl-CoA
-
cosubstrate gentamicin C1a
0.0017
acetyl-CoA
-
cosubstrate tobramycin
0.0027
acetyl-CoA
pH 6.0, 37°C
0.0027
acetyl-CoA
recombinant His-tagged enzyme, pH 6.0, 37°C
0.0154
acetyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
0.0362
acetyl-CoA
25°C, pH not specified in the publication
0.086
acetyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.17
acetyl-CoA
-
cosubstrate neomycin B, pH 7.6, 25°C
0.00096
amikacin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0021
amikacin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0716
amikacin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
11.07
amikacin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0092
dibekacin
pH 6.0, 37°C
0.0092
dibekacin
recombinant His-tagged enzyme, pH 6.0, 37°C
0.0029
gentamicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0046
gentamicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0189
gentamicin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.002
gentamicin C1
-
pH 7.6, 25°C
0.002
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a
0.0033
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.0048
kanamycin A
-
pH 7.6, 25°C
0.0048
kanamycin A
pH 7.6, 25°C
0.0048
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a
0.0055
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0091
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.0099
kanamycin A
-
pH 6.6, with acetyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.0111
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0135
kanamycin A
-
pH 6.6, with n-propionyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.238
kanamycin A
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0026
kanamycin B
-
pH 7.6, 25°C
0.0026
kanamycin B
pH 7.6, 25°C
0.0138
kanamycin B
pH 6.0, 37°C
0.0138
kanamycin B
recombinant His-tagged enzyme, pH 6.0, 37°C
0.0802
kanamycin B
-
pH 7.6, 25°C
0.234
malonyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
0.477
malonyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0012
neomycin B
-
pH 7.6, 25°C
0.0031
neomycin B
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0148
neomycin B
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.00015
paromomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0033
paromomycin
-
pH 7.6, 25°C
0.0023
ribostamycin
-
pH 7.6, 25°C
0.0031
ribostamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.00057
sisomicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.000724
sisomicin
-
pH 7.2, 34°C
0.0015
sisomicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.015
sisomicin
-
pH 7.6, 25°C
0.00033
sisomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0015
sisomycin
-
pH 7.6, 25°C
0.0015
sisomycin
pH 7.6, 25°C
0.0013
tobramycin
-
pH 7.6, 25°C
0.0013
tobramycin
pH 7.6, 25°C
0.00142
tobramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.0027
tobramycin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.0054
tobramycin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.106
tobramycin
-
pH 7.6, 25°C
additional information
additional information
-
kinetic pattern
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
61
apramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
3.5
butirosin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.3
butyryl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
9.7
gentamicin C1
-
pH 7.6, 25°C
18.4
gentamicin C2
-
pH 7.6, 25°C
40
gentamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
33.8
lividomycin A
-
pH 7.6, 25°C
10.2
n-propionyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
34
neomycin E
pH 7.6, 25°C
32
netilmicin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
33
propionyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.24
acetyl-CoA
pH 6.0, 37°C
0.24
acetyl-CoA
recombinant His-tagged enzyme, pH 6.0, 37°C
2.2
acetyl-CoA
25°C, pH not specified in the publication
10.5
acetyl-CoA
-
cosubstrate neomycin B, pH 7.6, 25°C
39
acetyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
39.4
acetyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
0.124
amikacin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.126
amikacin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.146
amikacin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.5
amikacin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.17
dibekacin
pH 6.0, 37°C
0.17
dibekacin
recombinant His-tagged enzyme, pH 6.0, 37°C
0.041
gentamicin
-
pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b
0.123
gentamicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.182
gentamicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.012
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a
0.017
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a
0.044
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.134
kanamycin A
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.144
kanamycin A
-
pH 6.6, with n-propionyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
0.163
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps
0.3
kanamycin A
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
0.559
kanamycin A
-
pH 6.6, with acetyl-CoA, untagged enzyme expressed from vector Int-pET19b-pps
51
kanamycin A
pH 7.6, 25°C
51.4
kanamycin A
-
pH 7.6, 25°C
80
kanamycin A
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.23
kanamycin B
pH 6.0, 37°C
0.23
kanamycin B
recombinant His-tagged enzyme, pH 6.0, 37°C
14.5
kanamycin B
-
pH 7.6, 25°C
54.5
kanamycin B
-
pH 7.6, 25°C
55
kanamycin B
pH 7.6, 25°C
5.7
malonyl-CoA
-
cosubstrate kanamycin A, pH 7.6, 25°C
9
malonyl-CoA
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
10
neomycin
pH 7.6, 25°C
60
neomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.076
neomycin B
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.188
neomycin B
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
9.5
neomycin B
-
pH 7.6, 25°C
15
paromomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
33.6
paromomycin
-
pH 7.6, 25°C
23.5
ribostamycin
-
pH 7.6, 25°C
24
ribostamycin
pH 7.6, 25°C
146
ribostamycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.121
sisomicin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.173
sisomicin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
24.5
sisomicin
-
pH 7.6, 25°C
46
sisomycin
pH 7.6, 25°C
46.3
sisomycin
-
pH 7.6, 25°C
51
sisomycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
0.089
tobramycin
-
pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b
0.179
tobramycin
-
pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b
43.5
tobramycin
-
pH 7.6, 25°C
47.8
tobramycin
-
pH 7.6, 25°C
48
tobramycin
pH 7.6, 25°C
162
tobramycin
in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C
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.
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.
Davies, J.; O'Connor, S.
Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin
Antimicrob. Agents Chemother.
14
69-72
1978
Arizona sp., Escherichia coli, Klebsiella pneumoniae
brenda
Wolf, E.; Vassilev, A.; Makino, Y.; Sali, A.; Nakatani, Y.; Burley, S.K.
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
Cell
94
439-449
1998
Serratia marcescens
brenda
Ishikawa, J.; Sunada, A.; Oyama, R.; Hotta, K.
Identification and characterization of the point mutation which affects the transcription level of the chromosomal 3-N-acetyltransferase gene of Streptomyces griseus SS-1198
Antimicrob. Agents Chemother.
44
437-440
2000
Streptomyces griseus
brenda
Tsuchizaki, N.; Hamadal, M.; Hotta, K.
Rapid characterization by colony direct PCR of distribution specificity in Streptomyces of kan gene encoding a specific aminoglycoside-3-N-acetyltransferase
Actinomycetologica
15
23-29
2001
Streptomyces griseus (Q54216)
-
brenda
Riccio, M.L.; Docquier, J.D.; Dell'Amico, E.; Luzzaro, F.; Amicosante, G.; Rossolini, G.M.
Novel 3-N-aminoglycoside acetyltransferase gene, aac(3)-Ic, from a Pseudomonas aeruginosa integron
Antimicrob. Agents Chemother.
47
1746-1748
2003
Pseudomonas aeruginosa (Q83V16), Pseudomonas aeruginosa
brenda
Biddlecome, S.; Haas, M.; Davies, J.; Rane, D.F.; Daniels, P.J.L.
Enzymatic modification of aminoglycoside antibiotics: a new 3-N-acetylating enzyme from a Pseudomonas aeruginosa isolate
Antimicrob. Agents Chemother.
9
951-955
1976
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas aeruginosa Travers PST, Escherichia coli R135/C600
brenda
Angelatou, F.; Litsas, S.B.; Kontomichalou, P.
Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa
J. Antibiot.
35
235-244
1982
Pseudomonas aeruginosa
brenda
Williams, J.W.; Northrop, D.B.
Kinetic mechanisms of gentamicin acetyltransferase I. Antibiotic-dependent shift from rapid to nonrapid equilibrium random mechanisms
J. Biol. Chem.
253
5902-5907
1978
Escherichia coli, Escherichia coli C600
brenda
Bongaerts, Ger P.A.; Vliegenthart, John S.
Effect of aminoglycoside concentration on reaction rates of aminoglycoside-modifying enzymes
Antimicrob. Agents Chemother.
32
740-746
1988
Escherichia coli, Escherichia coli JR88
brenda
Gomez-Lus, R.; Gomez-Lus, S.; Goni, M.P.; Rivera, M.J.; Martin, C.; Rubio-Calvo, M.C.
Stability of dactimicin to aminoglycoside-modifying enzymes produced by 341 bacterial clinical isolates
Drugs Exp. Clin. Res.
15
129-132
1989
Escherichia coli
brenda
Levings, R.S.; Partridge, S.R.; Lightfoot, D.; Hall, R.M.; Djordjevic, S.P.
New integron-associated gene cassette encoding a 3-N-aminoglycoside acetyltransferase
Antimicrob. Agents Chemother.
49
1238-1241
2005
Salmonella enterica subsp. enterica serovar Kentucky (Q6S741)
brenda
Coombe, R.G.; George, A.M.
Purification and properties of an aminoglycoside acetyltransferase from Pseudomonas aeruginosa
Biochemistry
21
871-875
1982
Pseudomonas aeruginosa
brenda
Elbourne, L.D.; Hall, R.M.
Gene cassette encoding a 3-N-aminoglycoside acetyltransferase in a chromosomal integron. Comments
Antimicrob. Agents Chemother.
50
2270-2271
2006
Saccharophagus degradans
brenda
Magalhaes, M.L.; Blanchard, J.S.
The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli
Biochemistry
44
16275-16283
2005
Escherichia coli (Q306W4), Escherichia coli, Escherichia coli BL21(DE3) pLysS (Q306W4)
brenda
Welch, K.T.; Virga, K.G.; Whittemore, N.A.; Oezen, C.; Wright, E.; Brown, C.L.; Lee, R.E.; Serpersu, E.H.
Discovery of non-carbohydrate inhibitors of aminoglycoside-modifying enzymes
Bioorg. Med. Chem.
13
6252-6263
2005
Homo sapiens
brenda
Subba, B.; Kharel, M.K.; Lee, H.C.; Liou, K.; Kim, B.G.; Sohng, J.K.
The ribostamycin biosynthetic gene cluster in Streptomyces ribosidificus: comparison with butirosin biosynthesis
Mol. Cell
20
90-96
2005
Streptomyces ribosidificus (Q4R0X5), Streptomyces ribosidificus
brenda
Green, K.D.; Chen, W.; Houghton, J.L.; Fridman, M.; Garneau-Tsodikova, S.
Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides
ChemBioChem
11
119-126
2010
Escherichia coli
brenda
Cabrera, R.; Ruiz, J.; Sanchez-Cespedes, J.; Goni, P.; Gomez-Lus, R.; Jimenez de Anta, M.T.; Gascon, J.; Vila, J.
Characterization of the enzyme aac(3)-Id in a clinical isolate of Salmonella enterica serovar Haifa causing travelers diarrhea
Enferm. Infecc. Microbiol. Clin.
27
453-456
2009
Salmonella enterica
brenda
Norris, A.L.; Ozen, C.; Serpersu, E.H.
Thermodynamics and kinetics of association of antibiotics with the aminoglycoside acetyltransferase (3)-IIIb, a resistance-causing enzyme
Biochemistry
49
4027-4035
2010
Pseudomonas aeruginosa
brenda
Norris, A.L.; Serpersu, E.H.
Interactions of coenzyme A with the aminoglycoside acetyltransferase (3)-IIIb and thermodynamics of a ternary system
Biochemistry
49
4036-4042
2010
Pseudomonas aeruginosa
brenda
Galimand, M.; Fishovitz, J.; Lambert, T.; Barbe, V.; Zajicek, J.; Mobashery, S.; Courvalin, P.
AAC(3)-XI, a new aminoglycoside 3-N-acetyltransferase from Corynebacterium striatum
Antimicrob. Agents Chemother.
59
5647-5653
2015
Corynebacterium striatum, Corynebacterium striatum (A0A0K2X0F2), Corynebacterium striatum BM4687, Corynebacterium striatum BM4687 (A0A0K2X0F2)
brenda
Norris, A.L.; Nickels, J.; Sokolov, A.P.; Serpersu, E.H.
Protein dynamics are influenced by the order of ligand binding to an antibiotic resistance enzyme
Biochemistry
53
30-38
2014
Pseudomonas aeruginosa (Q51405)
brenda
Atasoy, A.R.; Ciftci, I.H.; Petek, M.
Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates
Int. J. Clin. Exp. Med.
8
2874-2880
2015
Acinetobacter baumannii (P29807)
brenda
Ung, K.; Alsarraf, H.; Olieric, V.; Kremer, L.; Blaise, M.
Crystal structure of the aminoglycosides N-acetyltransferase Eis2 from Mycobacteriumxa0abscessus
FEBS J.
286
4342-4355
2019
Mycobacteroides abscessus (B1MKV6), Mycobacteroides abscessus DSM 44196 (B1MKV6)
brenda
Garzan, A.; Willby, M.; Green, K.; Gajadeera, C.; Hou, C.; Tsodikov, O.; Posey, J.; Garneau-Tsodikova, S.
Sulfonamide-based inhibitors of aminoglycoside acetyltransferase Eis abolish resistance to kanamycin in Mycobacterium tuberculosis
J. Med. Chem.
59
10619-10628
2016
Mycobacterium tuberculosis (P9WFK7), Mycobacterium tuberculosis H37Rv (P9WFK7)
brenda
Kumar, P.; Selvaraj, B.; Serpersu, E.; Cuneo, M.
Encoding of promiscuity in an aminoglycoside acetyltransferase
J. Med. Chem.
61
10218-10227
2018
Pseudomonas aeruginosa (Q51405)
brenda
Kumar, P.; Serpersu, E.
Thermodynamics of an aminoglycoside modifying enzyme with low substrate promiscuity The aminoglycoside N3 acetyltransferase-VIa
Proteins
85
1258-1265
2017
Enterobacter cloacae
brenda