Overproduction and Substrate Specificity of 3-Isopropylmalate Dehydrogenase fromThiobacillus ferrooxidans | Zendy

H. Matsunami | Zendy; Hiroshi Kawaguchi | Zendy; Kenji Inagaki | Zendy; Tadashi Eguchi | Zendy; Shizuko Kakinuma | Zendy; Hidehiko Tanaka | Zendy

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Overproduction and Substrate Specificity of 3-Isopropylmalate Dehydrogenase fromThiobacillus ferrooxidans

Author(s) -

H. Matsunami,

Hiroshi Kawaguchi,

Kenji Inagaki,

Tadashi Eguchi,

Shizuko Kakinuma,

Hidehiko Tanaka

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.372

Subject(s) - thiobacillus ferrooxidans , thiobacillus , dehydrogenase , escherichia coli , enzyme , overproduction , biochemistry , plasmid , substrate (aquarium) , substrate specificity , biology , gene , microbiology and biotechnology , chemistry , bacteria , genetics , ecology

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.

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