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Purification of Fumarase from Corynebacterium glutamicum andInhibition by Substrate Analogs

Bulletin of the Faculty of Education, Yamaguchi University. Natural science Volume 56 Issue 2 Page 121-134
published_at 2005-12-20
C020056000202.pdf
[fulltext] 896 KB
Title
Corynebacterium glutamicumからのフマラーゼの精製と基質アナログ阻害
Purification of Fumarase from Corynebacterium glutamicum andInhibition by Substrate Analogs
Creators Genda Tomoko
Creators Watabe Shoji
Creators Ozaki Hachiro
Source Identifiers
Fumarase (EC 4.2.1.2) from Corynebacterium glutamicum (Breuibacterium 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 (GeneBank 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 in phosphate buffer, while 16, 19, and 17 in the non-phosphate buffers, respectively. Among amino acids and nucleotides tested ATP inhibited the enzyme. Substrate analogs, meso-tartrate, D-tartrate, and pyromellitate, inhibited the enzyme competitively, and D-malate in mixed-type.
Subjects
自然科学 ( Other)
Languages eng
Resource Type departmental bulletin paper
Publishers 山口大学教育学部
Date Issued 2005-12-20
File Version Version of Record
Access Rights open access
Relations
[ISSN]1349-810X
[NCID]AN00243950
Schools 教育学部