Chemical modification locates guanidinyl and carboxylate groups within the active site of prolidase.
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.
Mock
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WL
Department of Chemistry, University of Illinois, Chicago 60680-4348.
Zhuang
H
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D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000737:chemistry*; D001224:Aspartic Acid / Q000737:chemistry*; D001665:Binding Sites; D003028:CME-Carbodiimide / Q000031:analogs & derivatives*; D002234:Carbodiimides; D003432:Cross-Linking Reagents; D004150:Dipeptidases / Q000737:chemistry*; D005971:Glutamates / Q000737:chemistry*; D018698:Glutamic Acid; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D010658:Phenylglyoxal; D013329:Structure-Activity Relationship; D013552:Swine
D002234:Carbodiimides; D003432:Cross-Linking Reagents; D005971:Glutamates; C074111:N-cyclohexyl-N'-2-morpholinoethyl-carbodiimide-methyl-4-toluolsulfonate; D003028:CME-Carbodiimide; D001224:Aspartic Acid; D018698:Glutamic Acid; D001120:Arginine; D004150:Dipeptidases; C022449:proline dipeptidase; D010658:Phenylglyoxal