Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from Thiobacillus ferrooxidans.

Article abstract of DOI:10.1271/bbb.62.372

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.

Full text of DOI:10.1271/bbb.62.372

Bioscience, Biotechnology, and Biochemistry
ISSN: 0916-8451 (Print) 1347-6947 (Online) Journal homepage: http://www.tandfonline.com/loi/tbbb20
Overproduction and Substrate Specificity of 3-
Isopropylmalate Dehydrogenase from Thiobacillus
ferrooxidans
Hideyuki MATSUNAMI, Hiroshi KAWAGUCHI, Kenji INAGAKI, Tadashi EGUCHI,
Katsumi KAKINUMA & Hidehiko TANAKA
To cite this article: Hideyuki MATSUNAMI, Hiroshi KAWAGUCHI, Kenji INAGAKI, Tadashi
EGUCHI, Katsumi KAKINUMA & Hidehiko TANAKA (1998) Overproduction and Substrate
Specificity of 3-Isopropylmalate Dehydrogenase from Thiobacillus ferrooxidans , Bioscience,
Biotechnology, and Biochemistry, 62:2, 372-373, DOI: 10.1271/bbb.62.372
To link to this article: http://dx.doi.org/10.1271/bbb.62.372
Published online: 22 May 2014.
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Date: 10 June 2016, At: 21:28