Action on peptides by wheat carboxypeptidase |
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Authors: | H. Umetsu E. Ichishima |
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Affiliation: | Laboratory of Enzymology and Microbial Chemistry, Tokyo Nōkō University, Fuchu, Tokyo 183 Japan |
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Abstract: | A kinetic analysis has been performed with purified wheat carboxypeptidase by the use of N-acyl dipeptides, Z-Gly-Pro-Leu-Gly (Z = benzyloxycarbonyl), angiotensin II and bradykinin. The values of kcat were dramatically influenced by amino acid residues occupying the penultimate position from the carboxyl terminus of substrates. The structure of the substrate did not appreciably affect the Km values. |
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Keywords: | Gramineae wheat carboxypeptidase peptides kinetic parameters |
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