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.
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 gamma-glutamyl amino acids by the action of gamma-glutamylcyclotransferase is converted to glutamate, appears to function in the gamma-glutamyl cycle. 5-Oxoprolinase requires Mg(++) (or Mn(++)) and K(+) (or NH(4) (+)) for activity. The equilibrium is markedly in favor of glutamate formation at pH 7.8.
D000227:Adenine Nucleotides / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002247:Carbon Isotopes; D002845:Chromatography; D005971:Glutamates / Q000096:biosynthesis*; D006801:Humans; D007422:Intestines / Q000201:enzymology; D007668:Kidney / Q000187:drug effects / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D009206:Myocardium / Q000201:enzymology; D011188:Potassium / Q000494:pharmacology; D011760:Pyrrolidinones / Q000378:metabolism*; D051381:Rats; D012756:Sheep; D013154:Spleen / Q000201:enzymology; D013552:Swine
D000227:Adenine Nucleotides; D002247:Carbon Isotopes; D005971:Glutamates; D011760:Pyrrolidinones; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000581:Amidohydrolases; D008274:Magnesium; D011188:Potassium