Affiliation:
1. The Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QY, U.K.
Abstract
The specificity of the S1′ subsite of the proteolytic enzyme papain was investigated by studying the effect of l-α-amino acid amides on the enzyme-catalysed hydrolysis of N-benzyloxycarbonylglycine p-nitrophenyl ester and by determining the kinetic parameters for the enzyme-catalysed hydrolysis of some N-benzyloxycarbonylglycyl-l-amino acid amides. These studies showed that the S1′ subsite has a predilection for hydrophobic residues, in particular l-leucine and l-tryptophan. The specificity for these residues is manifest in both the binding and acylation steps. N-Benzyloxycarbonylglycine amide is not hydrolysed under comparable conditions, indicating that the amide group adjacent to and on the C-terminal side of the peptide bond about to be cleaved makes an important contribution to the rate of the papain-catalysed hydrolysis of peptides.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
39 articles.
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