Information on EC 4.3.2.7 - glutathione-specific gamma-glutamylcyclotransferase

for references in articles please use BRENDA:EC4.3.2.7
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.3.2.7
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RECOMMENDED NAME
GeneOntology No.
glutathione-specific gamma-glutamylcyclotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glutathione = L-cysteinylglycine + 5-oxo-L-proline
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5-oxo-L-proline metabolism
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Glutathione metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
glutathione gamma-glutamyl cyclotransferase (5-oxo-L-proline producing)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
gamma-glutamyl-L-alanine
5-oxo-L-proline + L-alanine
show the reaction diagram
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poor substrate
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-
?
glutathione
L-cysteinylglycine + 5-oxo-L-proline
show the reaction diagram
additional information
?
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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
glutathione
L-cysteinylglycine + 5-oxo-L-proline
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 3.7
glutathione
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 0.27
glutathione
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
gel filtration
22000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure
to 1.43 A resolution. The catalytic site is defined by a fortuitous benzoic acid molecule bound to the crystal structure
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli and Saccharomyces cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E116Q
mutation of putative catalytic glutamate residue, loss of activity
E115Q
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mutation of putative catalytic glutamate residue, loss of activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
higher levels of ChaC1 transcripts are present in all the tumorigenic cell lines examined