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Enzyme Nomenclature
Information on EC 1.21.3.10 - hercynylcysteine S-oxide synthase
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EC Tree
1.21.3.10 hercynylcysteine S-oxide synthaseIUBMB Comments
Requires Fe2+ for activity. The enzyme, found in fungal species, is part of a fusion protein that also has the the activity of EC 2.1.1.44, L-histidine Nalpha-methyltransferase. It is part of the biosynthesis pathway of ergothioneine. The enzyme can also use L-selenocysteine to produce hercynylselenocysteine, which can be converted to selenoneine.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.99.51
-
-
formerly
-
Egt-1
Egt1
egt1+
EgtB
ergothioneine biosynthesis protein 1
protein SPBC1604.01
SPBC1604.01
Egt-1
-
-
-
-
Egt1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
hercynine,L-cysteine:oxygen [S-(hercyn-2-yl)-L-cysteine S-oxide-forming]
Requires Fe2+ for activity. The enzyme, found in fungal species, is part of a fusion protein that also has the the activity of EC 2.1.1.44, L-histidine Nalpha-methyltransferase. It is part of the biosynthesis pathway of ergothioneine. The enzyme can also use L-selenocysteine to produce hercynylselenocysteine, which can be converted to selenoneine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
hercynine + L-selenocysteine + O2
S-(hercyn-2-yl)-L-selenocysteine S-oxide + H2O
-
hercynine i.e. Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, enzyme Egt1 has about 62fold greater specificity (kobs/Km) for L-cysteine relative to gamma-Glu-Cys
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, low activity
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, low activity
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, enzyme Egt1 has about 62fold greater specificity (kobs/Km) for L-cysteine relative to gamma-Glu-Cys
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Methylobacterium brachiatum NBRC 103629
-
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
the enzyme is part of the biosynthesis pathway of ergothioneine
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
hercynine i.e. Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
?
-
-
enzyme additionally accepts gamma-L-glutamyl-L-cysteine, i.e. reaction of EC 1.14.99.50
-
-
-
additional information
?
-
-
enzyme does not accept gamma-L-glutamyl-L-cysteine, substrate of EC 1.14.99.50
-
-
-
additional information
?
-
Methylobacterium brachiatum NBRC 103629
-
enzyme does not accept gamma-L-glutamyl-L-cysteine, substrate of EC 1.14.99.50
-
-
-
additional information
?
-
enzyme does not accept gamma-L-glutamyl-L-cysteine, substrate of EC 1.14.99.50
-
-
-
additional information
?
-
usage of three different assays, when histidine and cysteine are the substrates (cf. EC 1.14.99.52), kobs is at least 100fold less than the case using the Cys and hercynine combination, and when gamma-Glu-Cys and hercynine are the substrates (cf. EC 1.14.99.50), the activity is low compared to the native substrates, and when gamma-Glu-Cys and histidine are the substrates, similar to the case of histidine and cysteine combination, the rate is close to background level, overview
-
-
?
additional information
?
-
three different assay methods for enzyme activity determination: a 1H NMR assay of chemical shift of the imidazole hydrogen atoms, an oxygen consumption assay, and a 13C NMR assay to monitor the presence of other cysteine related oxygen consumption. Egt1 from Neurospora crassa prefers cysteine as substrate compared to gamma-L-glutamyl-L-cysteine, Egt1 has a 62fold greater specificity (kobs/Km) for L-cysteine relative to gamma-Glu-Cys
-
-
?
additional information
?
-
three different assay methods for enzyme activity determination: a 1H NMR assay of chemical shift of the imidazole hydrogen atoms, an oxygen consumption assay, and a 13C NMR assay to monitor the presence of other cysteine related oxygen consumption. Egt1 from Neurospora crassa prefers cysteine as substrate compared to gamma-L-glutamyl-L-cysteine, Egt1 has a 62fold greater specificity (kobs/Km) for L-cysteine relative to gamma-Glu-Cys
-
-
?
additional information
?
-
usage of three different assays, when histidine and cysteine are the substrates (cf. EC 1.14.99.52), kobs is at least 100fold less than the case using the Cys and hercynine combination, and when gamma-Glu-Cys and hercynine are the substrates (cf. EC 1.14.99.50), the activity is low compared to the native substrates, and when gamma-Glu-Cys and histidine are the substrates, similar to the case of histidine and cysteine combination, the rate is close to background level, overview
-
-
?
additional information
?
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
additional information
?
-
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
additional information
?
-
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
-
-
?
additional information
?
-
-
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
-
-
?
additional information
?
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
additional information
?
-
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, low activity
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
reaction of EC 1.14.99.50, low activity
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
the enzyme is part of the biosynthesis pathway of ergothioneine
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
?
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
additional information
?
-
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
additional information
?
-
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
-
protein conatains 0.92 iron per monomer. A mononuclear nonheme iron is coordinated by His62, His153, His157 and three water molecules in an octahedral arrangement
Fe2+
a non-heme iron enzyme, that contains about 0.90 Fe per Egt1 monomer
Fe2+
required for catalysis, the enzyme contains about 0.90 Fe per Egt1 monomer
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.68
gamma-L-glutamyl-L-cysteine
pH and temperature not specified in the publication
0.013
hercynine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
0.023
hercynine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
0.039
hercynine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
0.088
hercynine
-
pH not specified in the publication, temperature not specified in the publication
0.39
hercynine
with gamma-L-glutamyl-L-cysteine, pH and temperature not specified in the publication
0.39
hercynine
pH and temperature not specified in the publication, with gamma-L-glutamyl-L-cysteine
0.436
hercynine
with L-Cys, pH and temperature not specified in the publication
0.436
hercynine
pH and temperature not specified in the publication, with L-Cys
0.028
L-cysteine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
0.047
L-cysteine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
0.049
L-cysteine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
0.205
L-cysteine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.603
L-cysteine
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.461
gamma-L-glutamyl-L-cysteine
pH and temperature not specified in the publication
0.44
hercynine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.46
hercynine
with gamma-L-glutamyl-L-cysteine, pH and temperature not specified in the publication
0.46
hercynine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
0.46
hercynine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
0.461
hercynine
pH and temperature not specified in the publication, with gamma-L-glutamyl-L-cysteine
0.55
hercynine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
2.267
hercynine
pH and temperature not specified in the publication, with L-Cys
2.27
hercynine
with L-Cys, pH and temperature not specified in the publication
0.028
L-cysteine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
0.047
L-cysteine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
0.049
L-cysteine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
0.205
L-cysteine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2.267
L-cysteine
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
hercynine
-
pH not specified in the publication, temperature not specified in the publication
11.7
hercynine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
23.3
hercynine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
35
hercynine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
2.2
L-cysteine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
9.7
L-cysteine
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
11.2
L-cysteine
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
16.3
L-cysteine
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
distribution of NcEgt-1 homologues in fungi, overview. The enzyme homologues are present in all of the true fungal groups in which ergothioneine is identified: Mucoromycotina (i.e., Mucorales), Agaricomycotina (i.e., Agaricales, Boletales, and Cantharellales), Pucciniomycotina (i.e., Sporidiobolales), and the Pezizomycotina (i.e., Eurotiales, Glomerellales, Hypocreales, and Sordariales)
evolution
mug158+/SPBC1604.01 is a distant homologue of the mycobacterial EgtD and EgtB genes, encoding a single fusion protein. The Schizosaccharomyces pombe homologue utilizes cysteine as a substrate, rather than using gamma-glutamyl-cysteine, as in the case of the bacterial EgtB enzyme, EC 1.14.99.50
evolution
-
mug158+/SPBC1604.01 is a distant homologue of the mycobacterial EgtD and EgtB genes, encoding a single fusion protein. The Schizosaccharomyces pombe homologue utilizes cysteine as a substrate, rather than using gamma-glutamyl-cysteine, as in the case of the bacterial EgtB enzyme, EC 1.14.99.50
-
evolution
-
distribution of NcEgt-1 homologues in fungi, overview. The enzyme homologues are present in all of the true fungal groups in which ergothioneine is identified: Mucoromycotina (i.e., Mucorales), Agaricomycotina (i.e., Agaricales, Boletales, and Cantharellales), Pucciniomycotina (i.e., Sporidiobolales), and the Pezizomycotina (i.e., Eurotiales, Glomerellales, Hypocreales, and Sordariales)
-
malfunction
-
the DELTA egt1 deletion mutant shows a complete absence of ergothioneine and all its precursors
malfunction
no ergothioneine is formed in the egt1-knockout mutant strain of Neurospora crassa, the mutant conidia show higher sensitivity to tert-butyl hydroperoxide compared to the wild-type strain, phenotype, overview
malfunction
Egt1 knockout in Neurospora crassa makes the mutant much more sensitive to oxidative stress compared to wild-type
malfunction
-
Egt1 knockout in Neurospora crassa makes the mutant much more sensitive to oxidative stress compared to wild-type
-
malfunction
-
no ergothioneine is formed in the egt1-knockout mutant strain of Neurospora crassa, the mutant conidia show higher sensitivity to tert-butyl hydroperoxide compared to the wild-type strain, phenotype, overview
-
metabolism
the enzyme catalyzes a step in the ergothioneine biosynthetic pathway, with the oxidative C-S bond formation and the subsequent C-S bond cleavage reaction, which result in a net transfer of the sulfur atom form cysteine to histidine imidazole side-chain, overview. The fungus Neurospora crassa has a more concise ergothioneine biosynthetic pathway because its nonheme iron enzyme, Egt1, makes use of cysteine instead of gamma-Glu-Cys as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses
metabolism
the enzyme catalyzes a step in the ergothioneine, EGT, biosynthetic pathway
metabolism
the enzyme produces hercynylcysteine sulfoxide in the ergothioneine pathway. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis involves an intermediate compound, hercynylselenocysteine
metabolism
the fungus Neurospora crassa has a concise ergothioneine biosynthetic pathway, its nonheme iron enzyme Egt1 makes use of cysteine instead of gamma-Glu-Cys (like EgtB, EC 1.14.99.50) as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses. In Neuropsora crassa ergothioneine biosynthesis, there are reactions distinct from the pathway via EgtB: the oxidative C-S bond formation and the subsequent C-S bond cleavage reaction, which result in a net transfer of the sulfur atom form cysteine to histidine imidazole side-chain
metabolism
-
the enzyme produces hercynylcysteine sulfoxide in the ergothioneine pathway. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis involves an intermediate compound, hercynylselenocysteine
-
metabolism
-
the fungus Neurospora crassa has a concise ergothioneine biosynthetic pathway, its nonheme iron enzyme Egt1 makes use of cysteine instead of gamma-Glu-Cys (like EgtB, EC 1.14.99.50) as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses. In Neuropsora crassa ergothioneine biosynthesis, there are reactions distinct from the pathway via EgtB: the oxidative C-S bond formation and the subsequent C-S bond cleavage reaction, which result in a net transfer of the sulfur atom form cysteine to histidine imidazole side-chain
-
metabolism
-
the enzyme catalyzes a step in the ergothioneine biosynthetic pathway, with the oxidative C-S bond formation and the subsequent C-S bond cleavage reaction, which result in a net transfer of the sulfur atom form cysteine to histidine imidazole side-chain, overview. The fungus Neurospora crassa has a more concise ergothioneine biosynthetic pathway because its nonheme iron enzyme, Egt1, makes use of cysteine instead of gamma-Glu-Cys as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses
-
metabolism
-
the enzyme catalyzes a step in the ergothioneine, EGT, biosynthetic pathway
-
physiological function
the enzyme is essentially involved in ergothioneine biosynthesis, which enhances conidial survival and protects against peroxide toxicity during conidial germination, overview. Ergothioneine does not have discernible pleiotropic affects and does not appear to protect against either Cu2+ toxicity or superoxide in vivo
physiological function
contribution of gene egt1+ to oxidative stress response, but gene egt1+ might not be among the primary mechanisms that protect Schizosaccharomyces pombe from exogenous peroxide
physiological function
-
EgtB of Candidatus Chloracidobacterium thermophilum has both EgtB- and Egt1-type of activities, i.e. reactions of EC 1.14.99.50 and EC 1.21.3.10
physiological function
-
contribution of gene egt1+ to oxidative stress response, but gene egt1+ might not be among the primary mechanisms that protect Schizosaccharomyces pombe from exogenous peroxide
-
physiological function
-
the enzyme is essentially involved in ergothioneine biosynthesis, which enhances conidial survival and protects against peroxide toxicity during conidial germination, overview. Ergothioneine does not have discernible pleiotropic affects and does not appear to protect against either Cu2+ toxicity or superoxide in vivo
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EGT1_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
876
0
99025
Swiss-Prot
other Location (Reliability: 2)
EGT1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
773
0
89714
Swiss-Prot
other Location (Reliability: 1)
A0A1I4PM45_9HYPH
422
0
47259
TrEMBL
-
EGT1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
773
0
89714
Swiss-Prot
-
EGT1_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
876
0
99025
Swiss-Prot
other Location (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme, found in fungal species, is part of a fusion protein that also has the the activity of EC 2.1.1.44, L-histidine Nalpha-methyltransferase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.5 A resolution. Enzyme is a tetramer. The active site is located at the interface between the N- and C-terminal domains for each monomer where a mononuclear nonheme iron is coordinated by His62, His153, His157 and three water molecules in an octahedral arrangement
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A420Y
-
position is involved in controlling the reaction selectiviy. Mutant leads to an increased amount of side-reaction (cysteine dioxygenase activity)
D52L
-
mutation may disrupt the hydrogen bond between Asp52 and glutamyl group of substrate gamma-Glu-Cys, which in turn alters the substrate selectivity
D52L/A420Y
-
mutation tunes EgtB activity toward Egt1-type, i.e. reaction of EC 1.21.3.10
additional information
additional information
the NcDELTAEgt-1 enzyme knockout strain does not produce ergothioneine. The mutant strain is not pleiotropically affected in rate of hyphal elongation in Vogel's medium either with or without ammonium nitrate and in the rate of germination of macroconidia on Vogel's medium, the mutant is also not differently affected from the wild-type by menadione and cupric sulfate, but germination of NcDELTAEgt-1 conidia is significantly more sensitive to tert-butyl hydroperoxide than the wild-type, phenotype, overview
additional information
-
the NcDELTAEgt-1 enzyme knockout strain does not produce ergothioneine. The mutant strain is not pleiotropically affected in rate of hyphal elongation in Vogel's medium either with or without ammonium nitrate and in the rate of germination of macroconidia on Vogel's medium, the mutant is also not differently affected from the wild-type by menadione and cupric sulfate, but germination of NcDELTAEgt-1 conidia is significantly more sensitive to tert-butyl hydroperoxide than the wild-type, phenotype, overview
-
additional information
construction of an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt1+ deletion mutant, DELTAegt1, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX) leading to absence of all ergothioneine pathway intermediates and ergothioneine itself in DELTAegt1. Employment of three versions of the nmt1 promoter plasmid with increasing strength of expression and constructed three strains P81nmt1-egt1+, P41nmt1-egt1+, and P3nmt1-egt1+, respectively. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells. No sensitivity or resistance of the mutant strains to oxidative stress compared to wild-type 972 strain
additional information
-
construction of an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt1+ deletion mutant, DELTAegt1, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX) leading to absence of all ergothioneine pathway intermediates and ergothioneine itself in DELTAegt1. Employment of three versions of the nmt1 promoter plasmid with increasing strength of expression and constructed three strains P81nmt1-egt1+, P41nmt1-egt1+, and P3nmt1-egt1+, respectively. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells. No sensitivity or resistance of the mutant strains to oxidative stress compared to wild-type 972 strain
additional information
-
construction of an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt1+ deletion mutant, DELTAegt1, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX) leading to absence of all ergothioneine pathway intermediates and ergothioneine itself in DELTAegt1. Employment of three versions of the nmt1 promoter plasmid with increasing strength of expression and constructed three strains P81nmt1-egt1+, P41nmt1-egt1+, and P3nmt1-egt1+, respectively. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells. No sensitivity or resistance of the mutant strains to oxidative stress compared to wild-type 972 strain
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene egt1+, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic tree
gene egt1, Egt1 recombinant overexpression from vector pASK-IBA3+ in Escherichia coli
gene egt1, overexpression in Escherichia coli strain BL21(DE3) from pASK-IBA3+ vector
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
biotechnology
the Neurospora crassa ergothioneine biosynthetic pathway may be a more suitable platform than the mycobacterial one for ergothioneine production through metabolic engineering because the ergothioneine and glutathione biosynthetic pathways are uncoupled and they do not compete with each other anymore in Neurospora crassa
biotechnology
-
the Neurospora crassa ergothioneine biosynthetic pathway may be a more suitable platform than the mycobacterial one for ergothioneine production through metabolic engineering because the ergothioneine and glutathione biosynthetic pathways are uncoupled and they do not compete with each other anymore in Neurospora crassa
-
synthesis
the ergothioneine biosynthetic pathway (EgtA-EgtE catalysis) provides an opportunity for ergothioneine production through metabolic engineering
synthesis
expression of EGT1 from Neurospora crassa and EGT2 from Claviceps purpurea in Yarrowia lipolytica to obtain 158 mg/l of ergothioneine in small-scale cultivation. An additional copy of each gene improves the titer to 205 mg/l. A phosphate-limited fed-batch fermentation in 1 l bioreactors yields 1.63 g/l ergothioneine in 220 h
synthesis
overexpression of the Egt-1 and -2 genes of Neurospora crassa in Aspergillus oryzae produces ergothioneine (231.0 mg/kg of media), with significant amounts of hercynine (32.7 mg/kg) accumulating in the culture
synthesis
-
overexpression of the Egt-1 and -2 genes of Neurospora crassa in Aspergillus oryzae produces ergothioneine (231.0 mg/kg of media), with significant amounts of hercynine (32.7 mg/kg) accumulating in the culture
-
synthesis
-
expression of EGT1 from Neurospora crassa and EGT2 from Claviceps purpurea in Yarrowia lipolytica to obtain 158 mg/l of ergothioneine in small-scale cultivation. An additional copy of each gene improves the titer to 205 mg/l. A phosphate-limited fed-batch fermentation in 1 l bioreactors yields 1.63 g/l ergothioneine in 220 h
-
synthesis
-
the ergothioneine biosynthetic pathway (EgtA-EgtE catalysis) provides an opportunity for ergothioneine production through metabolic engineering
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pluskal, T.; Ueno, M.; Yanagida, M.
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system
PLoS One
9
e97774
2014
Schizosaccharomyces pombe
brenda
Bello, M.; Barrera-Perez, V.; Morin, D.; Epstein, L.
The Neurospora crassa mutant NcDELTAEgt-1 identifies an ergothioneine biosynthetic gene and demonstrates that ergothioneine enhances conidial survival and protects against peroxide toxicity during conidial germination
Fungal Genet. Biol.
49
160-172
2012
no activity in Candida albicans, no activity in Saccharomyces cerevisiae, no activity in Pichia ssp., no activity in Bremia lactucae, Neurospora crassa (Q7RX33), Neurospora crassa ATCC 24698 (Q7RX33)
brenda
Hu, W.; Song, H.; Sae Her, A.; Bak, D.W.; Naowarojna, N.; Elliott, S.J.; Qin, L.; Chen, X.; Liu, P.
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway
Org. Lett.
16
5382-5385
2014
Neurospora crassa (Q7RX33), Neurospora crassa ATCC 24698 (Q7RX33)
brenda
Hu, W.; Song, H.; Sae Her, A.; Bak, D.W.; Naowarojna, N.; Elliott, S.J.; Qin, L.; Chen, X.; Liu, P.
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway
Org. Lett.
16
5382-5385
2014
Neurospora crassa (Q7RX33), Neurospora crassa ATCC 24698 (Q7RX33)
brenda
Pluskal, T.; Ueno, M.; Yanagida, M.
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system
PLoS ONE
9
e97774
2014
Schizosaccharomyces pombe (O94632), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972 (O94632)
brenda
Naowarojna, N.; Irani, S.; Hu, W.; Cheng, R.; Zhang, L.; Li, X.; Chen, J.; Zhang, Y.J.; Liu, P.
Crystal structure of the ergothioneine sulfoxide synthase from Candidatus Chloracidobacterium thermophilum and structure-guided engineering to modulate its substrate selectivity
ACS Catal.
9
6955-6961
2019
Chloracidobacterium thermophilum
brenda
Takusagawa, S.; Satoh, Y.; Ohtsu, I.; Dairi, T.
Ergothioneine production with Aspergillus oryzae
Biosci. Biotechnol. Biochem.
83
181-184
2019
Neurospora crassa (Q7RX33), Neurospora crassa, Neurospora crassa DSM 1257 (Q7RX33)
brenda
van der Hoek, S.A.; Rusnak, M.; Jacobsen, I.H.; Martinez, J.L.; Kell, D.B.; Borodina, I.
Engineering ergothioneine production in Yarrowia lipolytica
FEBS Lett.
596
1356-1364
2022
Neurospora crassa (Q7RX33), Neurospora crassa DSM 1257 (Q7RX33)
brenda
Kamide, T.; Takusagawa, S.; Tanaka, N.; Ogasawara, Y.; Kawano, Y.; Ohtsu, I.; Satoh, Y.; Dairi, T.
High production of ergothioneine in Escherichia coli using the sulfoxide synthase from Methylobacterium strains
J. Agric. Food Chem.
68
6390-6394
2020
Methylobacterium brachiatum, Methylobacterium pseudosasicola (A0A1I4PM45), Methylobacterium brachiatum NBRC 103629
brenda
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Release 2023.1 (January 2023)
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