5-oxoprolinase (ATP-hydrolysing)

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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 $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 3.5.2.9
BRENDA references for 3.5.2.9 (Recommended.)
PubMed references for 3.5.2.9
PubMed Central references for 3.5.2.9
Google Scholar references for 3.5.2.9
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: 2982–5. doi:10.1073/pnas.68.12.2982. PMID 5289242.