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Enzyme Nomenclature
Information on EC 1.14.99.51 - hercynylcysteine S-oxide synthase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.99.51
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RECOMMENDED NAME
GeneOntology No.
hercynylcysteine S-oxide synthase
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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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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
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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)
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malfunction
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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
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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
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metabolism
the enzyme catalyzes a step in the ergothioneine, EGT, biosynthetic pathway
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
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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
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metabolism
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the enzyme catalyzes a step in the ergothioneine, EGT, biosynthetic pathway
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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
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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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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
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hercynine i.e. Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
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-
?
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
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-
?
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
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-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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the enzyme is part of the biosynthesis pathway of ergothioneine
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-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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hercynine i.e. Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
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-
?
additional information
?
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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
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additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Q7RX33
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Q7RX33
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Q7RX33
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-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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the enzyme is part of the biosynthesis pathway of ergothioneine
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
a non-heme iron enzyme, that 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
0.603
L-cysteine
pH and temperature not specified in the publication
0.39
hercynine
with gamma-L-glutamyl-L-cysteine, pH and temperature not specified in the publication
0.436
hercynine
with L-Cys, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.46
hercynine
Neurospora crassa
Q7RX33
with gamma-L-glutamyl-L-cysteine, pH and temperature not specified in the publication
2.27
hercynine
Neurospora crassa
Q7RX33
with L-Cys, pH and temperature not specified in the publication
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene egt1, overexpression in Escherichia coli strain BL21(DE3) from pASK-IBA3+ vector
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.51)
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