Increase in activity for the C-terminal Pro-X bond by site-directed mutagenesis of Gly137 to Ala in carboxypeptidase Z.
作者信息
Ratanakhanokchai K, Lee B R, Kobayashi Y, Takeuchi M
机构信息
Laboratory of Molecular Biology and Microbial Chemistry, Tokyo University of Agriculture and Technology, Japan.
出版信息
Biosci Biotechnol Biochem. 1996 Mar;60(3):496-7. doi: 10.1271/bbb.60.496.
PMID:8901112
Abstract
A mutant carboxypeptidase Z from Absidia zychae in which Gly137 was replaced by Ala by site-directed mutagenesis was constructed and expressed in Saccharomyces cerevisiae YPH250. The mutant enzyme hydrolyzed C-terminal Pro-X bonds (X = amino acid) more efficiently than the wild-type enzyme and sequentially released amino acids from the C-termini of oligopeptides.
摘要
Zotero 插件