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Information on EC 4.3.2.7 - glutathione-specific gamma-glutamylcyclotransferase and Organism(s) Homo sapiens

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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:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
?
additional information
?
-
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
3.7
glutathione
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
glutathione
pH 8.0, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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
isoform ChaC2 degrades glutathione at lower efficiency than its ChaC1 homologue
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHAC1_HUMAN
222
0
24418
Swiss-Prot
other Location (Reliability: 2)
CHAC2_HUMAN
184
0
20875
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 22000, SDS-PAGE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
higher levels of ChaC1 transcripts are present in all the tumorigenic cell lines examined
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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