Abstract
3-Isopropylmalate dehydrogenase was purified to homogeneity from the acidophilic autotroph Thiobacillus thiooxidans. The native enzyme was a dimer of molecular weight 40,000. The apparent Km values for 3-isopropylmalate and NAD+ were estimated to be 0.13 mM and 8.7 mM, respectively. The optimum pH for activity was 9.0 and the optimum temperature was 65°C. The properties of the enzyme were similar to those of the Thiobacillus ferrooxidans enzyme, expect for substrate specificity. T. thiooxidans 3-isopropylmalate dehydrogenase could not utilize malate as a substrate.
| Original language | English |
|---|---|
| Pages (from-to) | 459-461 |
| Number of pages | 3 |
| Journal | Journal of Bioscience and Bioengineering |
| Volume | 90 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - Jan 1 2000 |
Keywords
- 3-isopropylmalate dehydrogenase
- Purification
- Thiobacillus thiooxidans
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
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Cite this
Kawaguchi, H., Inagaki, K., Matsunami, H., Nakayama, Y., Tano, T., & Tanaka, H. (2000). Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans. Journal of Bioscience and Bioengineering, 90(4), 459-461. https://doi.org/10.1016/S1389-1723(01)80020-7