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

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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.

Original language	English
Pages (from-to)	473-477
Number of pages	5
Journal	Applied Microbiology and Biotechnology
Volume	38
Issue number	4
DOIs	https://doi.org/10.1007/BF00242940
Publication status	Published - 01-1993
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Applied Microbiology and Biotechnology

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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 - Inoue, Yoshiharu

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

Abstract

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