Information on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Mycobacterium

EC NUMBER
COMMENTARY hide
1.14.99.50
-
RECOMMENDED NAME
GeneOntology No.
gamma-glutamyl hercynylcysteine S-oxide synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hercynine + gamma-L-glutamyl-L-cysteine + O2 = gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ergothioneine biosynthesis I (bacteria)
-
-
Histidine metabolism
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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 + N-glutaryl cysteine + O2
N-glutaryl-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
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
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
binding structure, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
required for enzyme stability
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene egtB, recombinant expression in Escherichia coli
recombinant overexpression of Strep-tagged enzyme in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (742 entries)
Please use the Sequence Search for a specific query.