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

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

doi:10.1016/S1572-4409(99)80097-2

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 journal › Article

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 K_m 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	https://doi.org/10.1016/S1572-4409(99)80097-2
Publication status	Published - 1999

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ASJC Scopus subject areas

Industrial and Manufacturing Engineering
Geotechnical Engineering and Engineering Geology

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Kawaguchi, H., Inagaki, K., Matsunami, H., Nakayama, Y., Tano, T., & Tanaka, H. (1999). Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans. Process Metallurgy, 9(C), 97-103. https://doi.org/10.1016/S1572-4409(99)80097-2

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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.",

author = "H. Kawaguchi and Kenji Inagaki and H. Matsunami and Y. Nakayama and T. Tano and H. Tanaka",

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AU - Kawaguchi, H.

AU - Inagaki, Kenji

AU - Matsunami, H.

AU - Nakayama, Y.

AU - Tano, T.

AU - Tanaka, H.

PY - 1999

Y1 - 1999

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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.

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10.1016/S1572-4409(99)80097-2