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

Access to Document

10.1271/bbb.62.372

Cite this

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

@article{54af3fb114a4410f90a7ca3c5c5d8486,

title = "Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans",

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.",

keywords = "3-isopropylmalate dehydrogenase, Leub, Overproduction, Substrate specificity, Thiobacillus ferrooxidans",

author = "Hideyuki Matsunami and Hiroshi Kawaguchi and Kenji Inagaki and Tadashi Eguchi and Katsumi Kakinuma and Hidehiko Tanaka",

year = "1998",

doi = "10.1271/bbb.62.372",

language = "English",

volume = "62",

pages = "372--373",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "2",

}

TY - JOUR

T1 - Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans

AU - Matsunami, Hideyuki

AU - Kawaguchi, Hiroshi

AU - Inagaki, Kenji

AU - Eguchi, Tadashi

AU - Kakinuma, Katsumi

AU - Tanaka, Hidehiko

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

KW - 3-isopropylmalate dehydrogenase

KW - Leub

KW - Overproduction

KW - Substrate specificity

KW - Thiobacillus ferrooxidans

UR - http://www.scopus.com/inward/record.url?scp=0031992853&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031992853&partnerID=8YFLogxK

U2 - 10.1271/bbb.62.372

DO - 10.1271/bbb.62.372

M3 - Article

C2 - 9532798

AN - SCOPUS:0031992853

VL - 62

SP - 372

EP - 373

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this