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 journalArticle

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 languageEnglish
Pages (from-to)372-373
Number of pages2
JournalBioscience, Biotechnology and Biochemistry
Volume62
Issue number2
DOIs
Publication statusPublished - Jan 1 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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