Chemical modification locates guanidinyl and carboxylate groups within the active site of prolidase

Abstract

Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline. The presence of arginine and carboxylate (aspartic/glutamic acid) residues at the active site of this metallodipeptidase may be inferred.