Purification and Characterization of Fumarase from Corynebacterium glutamicum

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概要

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• Fumarase (EC 4.2.1.2) from Corynebacterium glutamicum (Brevibacterium flavum) ATCC 14067 was purified to homogeneity. Its amino-terminal sequence (residues 1 to 30) corresponded to the sequence (residues 6 to 35) of the deduced product of the fumarase gene of C. glutamicum (GenBank accession no. BAB98403). The molecular mass of the native enzyme was 200 kDa. The protein was a homotetramer, with a 50-kDa subunit molecular mass. The homotetrameric and stable properties indicated that the enzyme belongs to a family of Class II fumarase. Equilibrium constants (Keq) for the enzyme reaction were determined at pH 6.0, 7.0, and 8.0, resulting in Keq=6.4, 6.1, and 4.6 respectively in phosphate buffer and in 16, 19, and 17 in non-phosphate buffers. Among the amino acids and nucleotides tested, ATP inhibited the enzyme competitively, or in mixed-type, depending on the buffer. Substrate analogs, meso-tartrate, D-tartrate, and pyromellitate, inhibited the enzyme competitively, and D-malate in mixed-type.

• 2006-05-23

著者

• Ozaki Hachiro

  Biological Institute Faculty Of Education Yamaguchi University

• Watabe Shoji

  Basic Laboratory Science Faculty Of Health Sciences Yamaguchi University School Of Medicine

• Genda Tomoko

  Biological Institute Faculty Of Education Yamaguchi University

関連論文

• Purification and Characterization of Fumarase from Corynebacterium glutamicum
• Activation of Mitochondrial ATP-Dependent Protease by Peptides and Proteins
• Purification and Characterization of Malate Dehydrogenase from Corynebacterium glutamicum(ENZYMOLOGY,PROTEIN ENGINEERING,AND ENZYME TECHNOLOGY)
• NOVEL DROSOPHILA PROTEINASE INHIBITOR HOMOLOGOUS TO THE PROREGIONS OF CYSTEINE PROTEINASES(Biochemistry,Abstracts of papers presented at the 76^ Annual Meeting of the Zoological Society of Japan)

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