Purification and Characterization of Malate Dehydrogenase from Corynebacterium glutamicum(ENZYMOLOGY,PROTEIN ENGINEERING,AND ENZYME TECHNOLOGY)

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概要

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• The malate dehydrogenase (MDH) (EC 1.1.1.37) from Corynebacterium glutamicum (Brevi-bacterium flavum) ATCC14067 was purified to homogeneity. Its amino-terminal sequence (residues 1 to 8) matched the sequence (residues 2 to 9) of the MDH from C. glutamicum (GenBank accession no. CAC83073). The molecular mass of the native enzyme was 130 kDa. The protein was a homotetramer, with a 33-kDa subunit molecular mass. The enzyme was almost equally active both for NADH and NADPH as coenzyme on the bases of the Acat values at pH 6.5 which is the optimum pH for the both coenzymes. Plotting of the logarithms of the 1/K_m, A_<cat>, and k_<cat>/K_m values with respect to oxalacetate against pH lead to speculation that imidazolium is possibly a functional group in the active center of the enzyme. Citrate activated the enzyme in the oxidation of malate to oxalacetate and inhibited it in the reverse reaction.

• 社団法人日本生物工学会の論文
• 2003-06-25

著者

• Ozaki H

  Department Of Materials Science And Engineering Tokyo Denki University

• GENDA TOMOKO

  Biological Institute, Faculty of Education, Yamaguchi University

• NAKAMATSU TSUYOSHI

  Biological Institute, Faculty of Education, Yamaguchi University

• OZAKI HACHIRO

  Department of Materials Science and Engineering, Tokyo Denki University

• Genda Tomoko

  Biological Institute Faculty Of Education Yamaguchi University

• Nakamatsu T

  Biological Institute Faculty Of Education Yamaguchi University

関連論文

• Glutamate Overproduction in Corynebacterium glutamicum Triggered by a Decrease in the Level of a Complex Comprising DtsR and a Biotin-containing Subunit
• Purification and Characterization of Fumarase from Corynebacterium glutamicum
• Purification and Characterization of Malate Dehydrogenase from Corynebacterium glutamicum(ENZYMOLOGY,PROTEIN ENGINEERING,AND ENZYME TECHNOLOGY)
• Molecular Cloning of a Novel Gene, dtsR, Which Rescues the Detergent Sensitivity of a Mutant Derived from Brevibacterium lactofermentum

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