Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans

Hiroshi Kawaguchi; Kenji Inagaki; Hideyuki Matsunami; Yumi Nakayama; Tatsuo Tano; Hidehiko Tanaka

doi:10.1016/S1389-1723(01)80020-7

Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans

Hiroshi Kawaguchi, Kenji Inagaki, Hideyuki Matsunami, Yumi Nakayama, Tatsuo Tano, Hidehiko Tanaka

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

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 K_m 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	https://doi.org/10.1016/S1389-1723(01)80020-7
Publication status	Published - 2000

Keywords

3-isopropylmalate dehydrogenase
Purification
Thiobacillus thiooxidans

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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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.",

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year = "2000",

doi = "10.1016/S1389-1723(01)80020-7",

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journal = "Journal of Bioscience and Bioengineering",

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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

Y1 - 2000

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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Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans

Abstract

Keywords

ASJC Scopus subject areas

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