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

H. Kawaguchi; K. 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, K. Inagaki, H. Matsunami, Y. Nakayama, T. Tano, H. Tanaka

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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 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

ASJC Scopus subject areas

Geotechnical Engineering and Engineering Geology
Industrial and Manufacturing Engineering

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title = "Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans",

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 K. Inagaki and H. Matsunami and Y. Nakayama and T. Tano and H. Tanaka",

year = "1999",

doi = "10.1016/S1572-4409(99)80097-2",

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T1 - Purification and characterization of 3-isopropylmalate dehydrogenase of acidophilic autotroph Thiobacillus thiooxidans

AU - Kawaguchi, H.

AU - Inagaki, K.

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.

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

Abstract

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