Characterization of γ-glutamyl kinase mutants from Saccharomyces cerevisiae

被引：6

作者：

Tatehashi, Yuki ^{[1
]}

Takagi, Hiroshi ^{[1
]}

机构：

[1] Nara Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300192, Japan

来源：

JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2013年 / 116卷 / 05期

关键词：

Saccharomyces cerevisiae; Yeast; gamma-Glutamyl kinase; Proline synthesis; PUA domain; PROLINE BIOSYNTHESIS; FEEDBACK INHIBITION; ENZYME; ACCUMULATION; TOLERANCE; PHOSPHATE; 5-KINASE;

D O I：

10.1016/j.jbiosc.2013.05.018

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We characterized the yeast gamma-glutamyl kinase important for proline biosynthesis. Asp154 and Ile150 were involved in the affinity with glutamate as well as proline. The Asp154Asn and Ile150Thr mutants had increased thermostability, in addition to desensitization to proline. Deletion of a C-terminal domain dramatically decreased the reaction rate and stability. (C) 2013, The Society for Biotechnology, Japan. All rights reserved.

引用

页码：576 / 579

页数：4

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