Information on EC 3.5.2.9 - 5-oxoprolinase (ATP-hydrolysing) and Organism(s) Homo sapiens

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This record set is specific for:
Homo sapiens


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.5.2.9
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RECOMMENDED NAME
GeneOntology No.
5-oxoprolinase (ATP-hydrolysing)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5-oxo-L-proline metabolism
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gamma-glutamyl cycle
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glutathione metabolism
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Glutathione metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
5-oxo-L-proline amidohydrolase (ATP-hydrolysing)
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CAS REGISTRY NUMBER
COMMENTARY hide
9075-46-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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the enzyme is involved in the gamma-glutamyl cycle, a six-enzyme cycle that represents the primary pathway for glutathione synthesis and degradation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
show the reaction diagram
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
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
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
show the reaction diagram
O14841
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-2-Oxothiazolidine-4-carboxylate
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competitive inhibitor
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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peripheral mononuclear cells
Manually annotated by BRENDA team
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normal and cancer tissues
Manually annotated by BRENDA team
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normal and cancer tissues
Manually annotated by BRENDA team
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normal and cancer tissues
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, no loss of activity detected
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA in pT7-7, subcloned into mammalian expression vector pRc/CMV, transfected into MCF7
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genotyping
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1241V
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naturally occuring mutation, leading to 5-oxoprolinase deficiency
G860R
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naturally occuring mutation, leading to 5-oxoprolinase deficiency
S323R
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naturally occuring mutation, leading to 5-oxoprolinase deficiency
V1089I
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naturally occuring mutation, not involved into 5-oxoprolinase deficiency
additional information
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in a yeast in vivo growth assay mutations S323R, G860R, and D1241V affect the activity of the enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine