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

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 - Jan 1 2000

Fingerprint

Keywords

3-isopropylmalate dehydrogenase
Purification
Thiobacillus thiooxidans

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

Cite this

Kawaguchi, H., Inagaki, K., Matsunami, H., Nakayama, Y., Tano, T., & Tanaka, H. (2000). Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans. Journal of Bioscience and Bioengineering, 90(4), 459-461. https://doi.org/10.1016/S1389-1723(01)80020-7

@article{163a6292ec354650b4eec2d4bb4002a7,

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

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.",

keywords = "3-isopropylmalate dehydrogenase, Purification, Thiobacillus thiooxidans",

author = "Hiroshi Kawaguchi and Kenji Inagaki and Hideyuki Matsunami and Yumi Nakayama and Tatsuo Tano and Hidehiko Tanaka",

year = "2000",

month = jan

day = "1",

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

language = "English",

volume = "90",

pages = "459--461",

journal = "Journal of Bioscience and Bioengineering",

issn = "1389-1723",

publisher = "The Society for Biotechnology, Japan",

number = "4",

}

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

UR - http://www.scopus.com/inward/record.url?scp=0034302032&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034302032&partnerID=8YFLogxK

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 -

Access to Document

10.1016/S1389-1723(01)80020-7