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Information on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase and Organism(s) Mycolicibacterium smegmatis and UniProt Accession A0R5N0

for references in articles please use BRENDA:EC1.14.99.50
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IUBMB Comments
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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This record set is specific for:
Mycolicibacterium smegmatis
UNIPROT: A0R5N0
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The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
sulfoxide synthase, 5-histidylcysteine sulfoxide synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hercynine oxygenase
UniProt
EgtB
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
-
the enzyme is part of the biosynthesis pathway of ergothioneine
-
-
?
additional information
?
-
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
-
the enzyme is part of the biosynthesis pathway of ergothioneine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
metabolism
-
the enzyme is part of the biosynthesis pathway of ergothioneine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
contruction of an EgtB homologue sequence similarity network using a BLAST e value cutoff
recombinant overexpression of Strep-tagged enzyme in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
the ergothioneine biosynthetic pathway (EgtA-EgtE catalysis) provides an opportunity for ergothioneine production through metabolic engineering
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seebeck, F.P.
In vitro reconstitution of Mycobacterial ergothioneine biosynthesis
J. Am. Chem. Soc.
132
6632-6633
2010
Mycolicibacterium smegmatis (A0R5N0)
Manually annotated by BRENDA team
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
Mycolicibacterium smegmatis
Manually annotated by BRENDA team
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
Mycolicibacterium smegmatis (A0R5N0), Mycolicibacterium smegmatis ATCC 700084 (A0R5N0)
Manually annotated by BRENDA team
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
Mycolicibacterium smegmatis (A0R5N0), Mycolicibacterium smegmatis ATCC 700084 (A0R5N0)
Manually annotated by BRENDA team