By-product analogues for bovine carboxypeptidase B.
A series of monocarboxylic and dicarboxylic acid sulfur-containing by-product analogues of lysine and arginine has been synthesized and tested as competitive inhibitors of bovine carboxypeptidase B. The most effective derivatives were guanidinoethylmercaptosuccinic acid and aminopropylmer-captosuccinic acid with Kis of 4 and 8 X 10(-6) M, respectively. Kinetics studies established the pure competitive nature of the inhibition. Mixed studies with the alkylating reagents bromoacetyl-D-arginine and bromoacetamidobutylguanidine established their efficiency in protecting the active-center glutamic acid and tyrosine of bovine carboxypeptidase B, respectively, from irreversible alkylation. Kinetic studies with bovine carboxypeptidase A and porcine carboxypeptidase B showed a lack of efficiency for A and high degree of efficiency for B.
D000818:Animals; D001667:Binding, Competitive; D002264:Carboxylic Acids / Q000494:pharmacology; D002268:Carboxypeptidases / Q000378:metabolism*; D002417:Cattle; D003998:Dicarboxylic Acids / Q000494:pharmacology; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology; D013329:Structure-Activity Relationship
D002264:Carboxylic Acids; D003998:Dicarboxylic Acids; D002268:Carboxypeptidases