1.14.99.50: gamma-glutamyl hercynylcysteine S-oxide synthase
This is an abbreviated version!
For detailed information about gamma-glutamyl hercynylcysteine S-oxide synthase, go to the full flat file.
Word Map on EC 1.14.99.50
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1.14.99.50
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egtbs
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ergothioneine
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ovoas
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ovothiols
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sulfur
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mycobacterium
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synthases
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nonheme
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proteobacteria
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carbon-sulfur
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chloracidobacterium
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iron-dependent
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dioxygenase
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thermophilum
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thermoresistibile
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sulfur-containing
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diatom
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thiolate
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o2-dependent
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synthesis
- 1.14.99.50
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egtbs
- ergothioneine
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ovoas
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ovothiols
- sulfur
- mycobacterium
- synthases
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nonheme
- proteobacteria
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carbon-sulfur
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chloracidobacterium
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iron-dependent
- dioxygenase
- thermophilum
- thermoresistibile
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sulfur-containing
- diatom
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thiolate
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o2-dependent
- synthesis
Reaction
Synonyms
5-histidylcysteine sulfoxide synthase, Cabther_A1318, EgtB, EgtBthermo, hercynine oxygenase, sulfoxide synthase
ECTree
1.14.99.50 gamma-glutamyl hercynylcysteine S-oxide synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase
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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 + N-glutaryl cysteine + O2
N-glutaryl-(hercyn-2-yl)-L-cysteine S-oxide + H2O
N-glutaryl cysteine is a 100fold less efficient sulfur donor for wild type EgtBthermo but a 10fold better substrate for mutant EgtBD416N than gamma-L-glutamyl-L-cysteine
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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sulfoxide incorporation at C2 by EgtB
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-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 + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
the enzyme is part of the biosynthesis pathway of ergothioneine
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
hercynine i.e. Nalpha,Nalpha,Nalpha-trimethyl-L-histidine. The enzyme is specific for both hercynine and gamma-L-glutamyl-L-cysteine. No activity with cysteine, N-acetylcysteine, or glutathione
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
the enzyme is extremely specific in terms of substrate specificity
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
the enzyme is extremely specific in terms of substrate specificity
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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-
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
i.e. N-alpha-trimethyl histidine
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
i.e. N-alpha-trimethyl histidine. Substrate binding mode, detailed overview
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?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
additional information
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enzyme additionally accepts L-cysteine, i.e. reaction of EC 1.21.3.10
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additional information
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enzyme additionally accepts L-cysteine, i.e. reaction of EC 1.21.3.10
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additional information
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no activity with L-cysteine and L-histdine
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?
additional information
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enzyme EgtB is extremely specific in terms of substrate specificity. Enzyme activity determination using : a 1H NMR assay of chemical shift of the imidazole hydrogen atoms
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?
additional information
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enzyme EgtB is extremely specific in terms of substrate specificity. Enzyme activity determination using : a 1H NMR assay of chemical shift of the imidazole hydrogen atoms
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?
additional information
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product formation is monitored by cation exchange HPLC using 20 mM phosphoric acid at pH 2 as a mobile phase, and EgtB substrates and products are quantified by 1H NMR, overview
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additional information
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product formation is monitored by cation exchange HPLC using 20 mM phosphoric acid at pH 2 as a mobile phase, and EgtB substrates and products are quantified by 1H NMR, overview
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