通过将羧肽酶Z中的Gly137定点突变为Ala来提高C末端Pro-X键的活性。
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
通过定点诱变构建了来自雅致犁头霉的一种突变羧肽酶Z，其中第137位甘氨酸被丙氨酸取代，并在酿酒酵母YPH250中表达。与野生型酶相比，该突变酶能更有效地水解C端脯氨酸-X键（X = 氨基酸），并从寡肽的C端依次释放氨基酸。
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