Functional analysis of the γ-glutamylcysteine synthetase of Escherichia coli B: effect of substitution of His-150 to Ala

Yoshiharu Inoue; Yoshitaka Iba; Hiroshi Yano; Kousaku Murata; Akira Kimura

doi:10.1007/BF00242940

Functional analysis of the γ-glutamylcysteine synthetase of Escherichia coli B: effect of substitution of His-150 to Ala

Yoshiharu Inoue
, Yoshitaka Iba
, Hiroshi Yano
, Kousaku Murata
, Akira Kimura

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

5 被引用数 (Scopus)

抄録

A high expression system of the γ-glutamylcysteine synthetase gene (gshl) of Escherichia coli B was constructed, and rapid purification of GSH-I was performed. The active site of GSH-I was analysed by chemical modification, and Lys, Arg and His residues seemed to be involved in the active site of the enzyme. Among them, His residues were substituted to Ala by site-directed mutagenesis, and His-150 was found to be essential for the activity of GSH-I.

本文言語	英語
ページ（範囲）	473-477
ページ数	5
ジャーナル	Applied Microbiology and Biotechnology
巻	38
号	4
DOI	https://doi.org/10.1007/BF00242940
出版ステータス	出版済み - 01-1993
外部発表	はい

All Science Journal Classification (ASJC) codes

バイオテクノロジー
応用微生物学とバイオテクノロジー

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10.1007/BF00242940

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abstract = "A high expression system of the γ-glutamylcysteine synthetase gene (gshl) of Escherichia coli B was constructed, and rapid purification of GSH-I was performed. The active site of GSH-I was analysed by chemical modification, and Lys, Arg and His residues seemed to be involved in the active site of the enzyme. Among them, His residues were substituted to Ala by site-directed mutagenesis, and His-150 was found to be essential for the activity of GSH-I.",

author = "Yoshiharu Inoue and Yoshitaka Iba and Hiroshi Yano and Kousaku Murata and Akira Kimura",

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AU - Iba, Yoshitaka

AU - Yano, Hiroshi

AU - Murata, Kousaku

AU - Kimura, Akira

PY - 1993/1

Y1 - 1993/1

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AB - A high expression system of the γ-glutamylcysteine synthetase gene (gshl) of Escherichia coli B was constructed, and rapid purification of GSH-I was performed. The active site of GSH-I was analysed by chemical modification, and Lys, Arg and His residues seemed to be involved in the active site of the enzyme. Among them, His residues were substituted to Ala by site-directed mutagenesis, and His-150 was found to be essential for the activity of GSH-I.

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ER -

Functional analysis of the γ-glutamylcysteine synthetase of Escherichia coli B: effect of substitution of His-150 to Ala

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