Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans

H. Kawaguchi, Kenji Inagaki, H. Matsunami, Y. Nakayama, T. Tano, H. Tanaka

Research output: Contribution to journalArticle

Abstract

3-Isopropylmalate dehydrogenase was purified to homogeneity from the acidophilic autotroph Thiobacillus thiooxidans. The native enzyme molecule is a dimer of molecular weight 40,000. The Km value for 3-isopropylmalate was estimated to be 0.13 mM and that for NAD+ 8.7 mM. The optimum pH and temperature for the activity are 9.0 and 65, respectively. The properties of the enzyme are similar to those of the Thiobacillus ferrooxidans enzymes, except for substrate specificity. T. ferrooxidans 3-isopropylmalate dehydrogenase is able to utilize alkyl-malate as substrate in addition to 3-isopropylmalate. However, T. thiooxidans 3-isopropylmalate is not able to utilize malate as a substrate.

Original languageEnglish
Pages (from-to)97-103
Number of pages7
JournalProcess Metallurgy
Volume9
Issue numberC
DOIs
Publication statusPublished - 1999

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Purification
purification
Enzymes
enzyme
substrate
Substrates
Dimers
homogeneity
Molecular weight
Molecules
Oxidoreductases
temperature
Temperature

ASJC Scopus subject areas

  • Industrial and Manufacturing Engineering
  • Geotechnical Engineering and Engineering Geology

Cite this

Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans. / Kawaguchi, H.; Inagaki, Kenji; Matsunami, H.; Nakayama, Y.; Tano, T.; Tanaka, H.

In: Process Metallurgy, Vol. 9, No. C, 1999, p. 97-103.

Research output: Contribution to journalArticle

Kawaguchi, H. ; Inagaki, Kenji ; Matsunami, H. ; Nakayama, Y. ; Tano, T. ; Tanaka, H. / Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans. In: Process Metallurgy. 1999 ; Vol. 9, No. C. pp. 97-103.
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AU - Tano, T.

AU - Tanaka, H.

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