Kinetic studies of carboxypeptidase Y. I. Kinetic parameters for the hydrolysis of synthetic substrates

Kinetic parameters for carboxypeptidase Y [EC 3.4.12.1], characterized as a nonspecific enzyme, are given for the hydrolysis of a series of acylated peptides, acylated amino acid esters, and amides. We confirmed that the enzyme released COOH-terminal proline and beta-alanine at an appreciable rate,...

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Bibliographic Details
Published inJournal of biochemistry (Tokyo) Vol. 77; no. 1?; pp. 69 - 79
Main Authors Hayashi, R, Bai, Y, Hata, T
Format Journal Article
LanguageEnglish
Published England 01.01.1975
Subjects
Anilides
Benzyl Compounds
Carboxypeptidases - metabolism
Dipeptides
Hydrogen-Ion Concentration
Kinetics
Oligopeptides
Osmolar Concentration
Phenols
Potassium Chloride - pharmacology
Saccharomyces cerevisiae - enzymology
Structure-Activity Relationship
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Summary:Kinetic parameters for carboxypeptidase Y [EC 3.4.12.1], characterized as a nonspecific enzyme, are given for the hydrolysis of a series of acylated peptides, acylated amino acid esters, and amides. We confirmed that the enzyme released COOH-terminal proline and beta-alanine at an appreciable rate, as well as neutral amino acids with aromatic and aliphatic side chains at a very high speed. The rates of hydrolysis of ester and amide substrates were compatible with those produced by chymotrypsin [EC 3.4.21.1]. Stereospecificity was also demonstrated by the failure to hydrolyze peptide, ester, amide, and anilide substrates containing a D-amino acid. The effects of pH, solvents, and salt concentrations on the kinetic parameters of hydrolysis of peptide and ester substrates are also described.
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ISSN:0021-924X