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
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
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.
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