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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Dec;68(12):2982–2985. doi: 10.1073/pnas.68.12.2982

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 γ-Glutamyl Cycle*

Paul Van Der Werf 1, Marian Orlowski 1, Alton Meister 1
PMCID: PMC389574  PMID: 5289242

Abstract

A new enzyme, 5-oxoprolinase, was found in rat kidney and in several other tissues; it catalyzes the conversion of 5-oxo-L-proline (L-5-oxo-pyrrolidine-2-carboxylic acid, L-2-pyrrolidone-5-carboxylic acid, L-pyroglutamic acid) to L-glutamic acid, with concomitant stoichiometric cleavage of ATP to ADP and orthophosphate. The reaction catalyzed by 5-oxoprolinase, in which 5-oxoproline formed from γ-glutamyl amino acids by the action of γ-glutamylcyclotransferase is converted to glutamate, appears to function in the γ-glutamyl cycle. 5-Oxoprolinase requires Mg++ (or Mn++) and K+ (or NH4+) for activity. The equilibrium is markedly in favor of glutamate formation at pH 7.8.

Keywords: kidney, amino-acid transport, pyroglutamic acid, 5-oxo-pyrrolidine-2-carboxylic acid

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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