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

H. Matsunami, H. Kawaguchi, Kenji Inagaki, T. Eguchi, K. Kakinuma, H. Tanaka

Research output: Contribution to journalArticle

5 Citations (Scopus)


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 languageEnglish
Pages (from-to)372-373
Number of pages2
JournalBioscience, Biotechnology and Biochemistry
Issue number2
Publication statusPublished - Feb 1998


ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

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