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Information on EC 4.3.2.7 - glutathione-specific gamma-glutamylcyclotransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32656

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.7 glutathione-specific gamma-glutamylcyclotransferase
IUBMB Comments
The enzyme, found in bacteria, fungi and animals, is specific for glutathione (cf. EC 4.3.2.9, gamma-glutamylcyclotransferase). The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P32656
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
chac1, chac2, glutathione-specific gamma-glutamylcyclotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CHAC
-
-
-
-
CHAC1
-
-
-
-
CHAC2
-
-
-
-
gamma-GCG
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
glutathione gamma-glutamyl cyclotransferase (5-oxo-L-proline producing)
The enzyme, found in bacteria, fungi and animals, is specific for glutathione (cf. EC 4.3.2.9, gamma-glutamylcyclotransferase). The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
SUBSTRATE
PRODUCT                       
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
-
-
-
?
gamma-glutamyl-L-alanine
5-oxo-L-proline + L-alanine
show the reaction diagram
-
poor substrate
-
-
?
glutathione
L-cysteinylglycine + 5-oxo-L-proline
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no substrate: gamma-glutamyl amino acids such as gamma-Glu-Cys, gamma-Glu-Met, gamma-Glu-His and gamma-Glu-Lys
-
-
?
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
glutathione
L-cysteinylglycine + 5-oxo-L-proline
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2
glutathione
-
pH 8, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
constitutively expressed
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
gamma-glutamyl cyclotransferase acts specifically to degrade glutathione but not other gamma-glutamyl peptides. The overexpression leads to glutathione depletion and enhanced apoptosis in yeast
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.43 A resolution. The catalytic site is defined by a fortuitous benzoic acid molecule bound to the crystal structure
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E115Q
-
mutation of putative catalytic glutamate residue, loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
development of a 5-oxoprolinase-coupled, sensitive, 5-oxoproline detection-based gamma-GCT assay. Development of an alternative assay that exploits the Cys-Gly generation from glutathione. Cys-Gly is converted into free cysteine and glycine with the help of Dug1p (a peptidase from Saccharomyces cerevisiae), followed by estimation of cysteine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, A.; Tikoo, S.; Maity, S.; Sengupta, S.; Sengupta, S.; Kaur, A.; Bachhawat, A.K.
Mammalian proapoptotic factor ChaC1 and its homologues function as gamma-glutamyl cyclotransferases acting specifically on glutathione
EMBO Rep.
13
1095-1101
2012
Mus musculus (Q8R3J5), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kaur, A.; Gautam, R.; Srivastava, R.; Chandel, A.; Kumar, A.; Karthikeyan, S.; Bachhawat, A.K.
ChaC2, an enzyme for slow turnover of cytosolic glutathione
J. Biol. Chem.
292
638-651
2017
Homo sapiens (Q8WUX2), Homo sapiens, Mus musculus (Q9CQG1), Mus musculus, Saccharomyces cerevisiae (P32656), Saccharomyces cerevisiae
Manually annotated by BRENDA team