Kinetics and Mechanism of Acetate Kinase from Bacillus stearothermophilus

JOURNAL OF CHEMICAL ENGINEERING OF JAPAN

Hiroshi Nakajima¹  Arief Widjaja²  Haruo Ishikawa²  Masahiro Shiroshima²  Ryoichi Tsurutani¹ 

[1] Biochemistry Department, Unitika Research and Development Center;Department of Chemical Engineering, University of Osaka Prefecture

关键词: Biochemical Engineering;    Allosteric Enzyme;    Random Bi Bi;    Reaction Rate;    ATP Regeneration;   

DOI  :  10.1252/jcej.28.517

来源: Maruzen Company Ltd

【 摘 要 】

References(18)Cited-By(8)The initial rates of ATP regeneration catalyzed by acetate kinase (ATP: acetate phosphotransferase; EC 2.7.2.1) from Bacillus stearothermophilus were measured under a wide range of MgADP–, acetyl phosphate, MgATP2– and acetate concentrations. The experimental results showed that the enzyme exhibited positive co-operativity for MgATP2– and no co-operativity for MgADP–, acetyl phosphate and acetate. Furthermore, the initial rates of the forward reaction, in which MgATP2– and acetate were produced from MgADP– and acetyl phosphate, were inhibited by MgATP2– and acetate, and those of the reverse reaction were inhibited by MgADP– and acetyl phosphate. The initial rate data were correlated well by using the rate equation derived based on the assumption that the reaction obeys the general reaction scheme based on the Random Bi Bi mechanism, and on the previous experimental result that the enzyme behaves like a dimeric enzyme, even though it is a tetrameric enzyme.

【 授权许可】

Unknown