Kinetic studies of carboxypeptidase Y. II.  Effects of substrate and product analogs on peptidase and esterase activities.
Reversible inhibition of the peptidase and esterase activities of CPase Y [EC 3.4.12.1] was investigated with substrate and product analogs known to be inhibitors or effectors of pancreatic carboxypeptidases A or B [EC 3.4.12.2 or 3]. L-Amino acids and NH2-blocked L-Amino acids showed competitive-type inhibition, whereas their D-enantiomers caused less inhibition than the L-enantiomers, and showed non-competitive or mixed-type inhibition. Some phenylalanine analogs, e.g. beta-phenylpropionic acid and t-cinnamic acid, were also reversible inhibitors of CPase Y. The type of these inhibitors and their K1 values were generally parallel for both the peptidase and esterase activities.
D000596:Amino Acids / Q000494:pharmacology; D001593:Benzyl Compounds / Q000494:pharmacology; D002268:Carboxypeptidases / Q000378:metabolism*; D004151:Dipeptides / Q000494:pharmacology; D004950:Esterases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007536:Isomerism; D007700:Kinetics; D010636:Phenols / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D000596:Amino Acids; D001593:Benzyl Compounds; D004151:Dipeptides; D010636:Phenols; D004950:Esterases; D002268:Carboxypeptidases