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. 1975 Sep;78(3):617-26.
doi: 10.1093/oxfordjournals.jbchem.a130948.

Kinetic studies of carboxypeptidase Y. III. Action on ester, amide, and anilide substrates and the effects of some environmental factors

Y Bai, R Hayashi, T Hata
Free article

Kinetic studies of carboxypeptidase Y. III. Action on ester, amide, and anilide substrates and the effects of some environmental factors

Y Bai et al. J Biochem. 1975 Sep.
Free article

Abstract

Kinetic parameters of carboxypeptidase Y are given for the hydrolyses of ester, amide, and anilide substrates. The kcat/Km values were compatible with those of chymotrypsin [EC 3.4.21.1] with a few exceptions. One ionizable group with a pK of around 5.8 was suggested to be involved in the free enzyme in hydrolyzing all the substrates, including peptide substrates. In addition, hydroxylaminolysis and the kinetic isotope effects of deuterium oxide indicated, with some reservations, a reaction mechanism which proceeds via the formation of an acyl intermediate.

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