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 language | English |
|---|---|
| Pages (from-to) | 372-373 |
| Number of pages | 2 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 62 |
| Issue number | 2 |
| Publication status | Published - Feb 1998 |
Fingerprint
ASJC Scopus subject areas
- Bioengineering
- Biotechnology
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Chemistry (miscellaneous)
- Applied Microbiology and Biotechnology
- Food Science
Cite this
Matsunami, H., Kawaguchi, H., Inagaki, K., Eguchi, T., Kakinuma, K., & Tanaka, H. (1998). Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from Thiobacillus ferrooxidans. Bioscience, Biotechnology and Biochemistry, 62(2), 372-373.