5-oxoprolinase (ATP-hydrolyzing) | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.2.9 | ||||||||
CAS no. | 9075-46-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 5-oxoprolinase (ATP-hydrolysing) (EC 3.5.2.9) is an enzyme that catalyzes the chemical reaction
- ATP + 5-oxo-L-proline + 2 H2O ADP + phosphate + L-glutamate
The 3 substrates of this enzyme are ATP, 5-oxo-L-proline, and H2O, whereas its 3 products are ADP, phosphate, and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5-oxo-L-proline amidohydrolase (ATP-hydrolysing). Other names in common use include pyroglutamase (ATP-hydrolysing), oxoprolinase, pyroglutamase, 5-oxoprolinase, pyroglutamate hydrolase, pyroglutamic hydrolase, L-pyroglutamate hydrolase, 5-oxo-L-prolinase, and pyroglutamase. This enzyme participates in glutathione metabolism.
References
- Van der Werf P, Orlowski M, Meister A (1971). "Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the -glutamyl cycle". Proc. Natl. Acad. Sci. U.S.A. 68 (12): 2982–5. doi:10.1073/pnas.68.12.2982. PMC 389574. PMID 5289242.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
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3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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