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Enzyme Nomenclature
Information on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase
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The expected taxonomic range for this enzyme is: Mycobacterium
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EC NUMBER 
COMMENTARY 
1.14.99.50
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RECOMMENDED NAME
GeneOntology No.
gamma-glutamyl hercynylcysteine S-oxide synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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hercynine + gamma-L-glutamyl-L-cysteine + O2 = gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
catalytic mechanism in which C-S bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-alpha-trimethyl histidine, proposed mechanism for EgtB-catalyzed C-S bond formation and sulfoxidation, overview
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
hercynine,gamma-L-glutamyl-L-cysteine:oxygen oxidoreductase [gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide-forming]
Requires Fe2+ for activity. The enzyme, found in bacteria, is specific for both hercynine and gamma-L-glutamyl-L-cysteine. It is part of the biosynthesis pathway of ergothioneine.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
enzyme EgtB catalyzes O2-dependent C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis
additional information
the two substrates and three histidine residues serve as ligands in an octahedral iron binding active site, enzyme structure analysis, detailed overview
evolution
enzyme EgtB represents a distinct enzyme class (sulfoxide synthases) with no relation to sulfur oxidizing or C-S bond-forming iron enzymes such as cysteine dioxygenase or isopenicillin synthase
evolution
the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
evolution
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the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
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metabolism
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the enzyme is part of the biosynthesis pathway of ergothioneine
metabolism
enzyme EgtB catalyzes O2-dependent C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis
metabolism
the enzyme catalyzes a step in the ergothioneine biosynthetic pathway, overview; the enzyme is involved in the ergothioneine biosynthesis catalyzing a direct four-electron oxidative process, coupling between hercynine and gamma-L-glutamyl-L-cysteine, overview
metabolism
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the enzyme catalyzes a step in the ergothioneine biosynthetic pathway, overview; the enzyme is involved in the ergothioneine biosynthesis catalyzing a direct four-electron oxidative process, coupling between hercynine and gamma-L-glutamyl-L-cysteine, overview
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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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the enzyme is part of the biosynthesis pathway of ergothioneine
-
-
?
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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-
-
?
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
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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-
?
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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 + 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
A0R5N0
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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
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
A0R5N0
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
A0R5N0
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
A0R5N0
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-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
A0R5N0
the enzyme is extremely specific in terms of substrate specificity
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
G7CFI3
i.e. N-alpha-trimethyl histidine
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
a non-heme iron enzyme, the two substrates and three histidine residues serve as ligands in an octahedral iron binding site, Glu140 rather than His51 is the metal ligand
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
the enzyme consists of an N-terminal DinB domain (residues 1-150), a two-stranded beta-sheet region (residues 151-210), and a C-terminal C-type lectin domain
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, as iron-bound holoenzyme, in complex with substrate gamma-glutamyl cysteine, N-alpha-dimethyl histidine and Mn2+ or with substrate N-alpha-trimethyl histidine and Fe2+, X-ray diffraction structure determination and analysis
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant overexpression of Strep-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D416N
site-directed mutagenesis, the mutation increases KM for gamma-glutamyl cysteine by 200fold but does not significantly change KM for N-alpha-trimethyl histidine or kcat compared to the wild-type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.50)
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