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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