Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans

Hideyuki Matsunami; Hiroshi Kawaguchi; Kenji Inagaki; Tadashi Eguchi; Katsumi Kakinuma; Hidehiko Tanaka

doi:10.1271/bbb.62.372

Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans

Hideyuki Matsunami, Hiroshi Kawaguchi, Kenji Inagaki, Tadashi Eguchi, Katsumi Kakinuma, Hidehiko Tanaka

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

5 Citations (Scopus)

Abstract

We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferrooxidans. E. coli harboring the plasmid we constructed, pKK leuB1, produced 17-fold the enzyme protein of the expression system previously used for purification. The substrate specificity of the enzyme was analyzed with synthetic (2R, 3S)-3-alkylmalates. The 3-isopropylmalate dehydrogenase of Thiobacillus ferrooxidans had broad specificity toward the alkylmalates.

Original language	English
Pages (from-to)	372-373
Number of pages	2
Journal	Bioscience, Biotechnology and Biochemistry
Volume	62
Issue number	2
DOIs	https://doi.org/10.1271/bbb.62.372
Publication status	Published - 1998

Keywords

3-isopropylmalate dehydrogenase
Leub
Overproduction
Substrate specificity
Thiobacillus ferrooxidans

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans. / Matsunami, Hideyuki; Kawaguchi, Hiroshi; Inagaki, Kenji; Eguchi, Tadashi; Kakinuma, Katsumi; Tanaka, Hidehiko.

In: Bioscience, Biotechnology and Biochemistry, Vol. 62, No. 2, 1998, p. 372-373.

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

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