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 language | English |
|---|---|
| Pages (from-to) | 97-103 |
| Number of pages | 7 |
| Journal | Process Metallurgy |
| Volume | 9 |
| Issue number | C |
| DOIs | |
| Publication status | Published - 1999 |
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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 journal › Article
}
TY - JOUR
T1 - Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans
AU - Kawaguchi, H.
AU - Inagaki, Kenji
AU - Matsunami, H.
AU - Nakayama, Y.
AU - Tano, T.
AU - Tanaka, H.
PY - 1999
Y1 - 1999
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77957101310&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77957101310&partnerID=8YFLogxK
U2 - 10.1016/S1572-4409(99)80097-2
DO - 10.1016/S1572-4409(99)80097-2
M3 - Article
AN - SCOPUS:77957101310
VL - 9
SP - 97
EP - 103
JO - Process Metallurgy
JF - Process Metallurgy
SN - 1572-4409
IS - C
ER -