| Literature DB >> 5415 |
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.Entities:
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Year: 1975 PMID: 5415 DOI: 10.1093/oxfordjournals.jbchem.a130948
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387