TY - JOUR
T1 - Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans
AU - Kawaguchi, Hiroshi
AU - Inagaki, Kenji
AU - Matsunami, Hideyuki
AU - Nakayama, Yumi
AU - Tano, Tatsuo
AU - Tanaka, Hidehiko
PY - 2000/1/1
Y1 - 2000/1/1
N2 - 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.
AB - 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.
KW - 3-isopropylmalate dehydrogenase
KW - Purification
KW - Thiobacillus thiooxidans
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U2 - 10.1016/S1389-1723(01)80020-7
DO - 10.1016/S1389-1723(01)80020-7
M3 - Article
C2 - 16232891
AN - SCOPUS:0034302032
VL - 90
SP - 459
EP - 461
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 4
ER -