Propionyl‐coenzyme A synthetases of Ralstonia solanacearum and Salmonella choleraesuis display atypical kinetics

FEBS Letters

Rajashekhara, Eranna¹  Watanabe, Kazuya¹ 

[1]Laboratory of Applied Microbiology, Marine Biotechnology Institute, 3-75-1 Heita, Kamaishi-shi 026-0001, Iwate-ken, Japan

关键词: Propionyl-CoA synthetase;    Kinetics;    Autoactivation;    Substrate inhibition;    Ralstonia;    Salmonella;    PCS;    propionyl-coenzyme A synthetase;    ACS;    acetyl-coenzyme A synthetase;    PCR;    polymerase chain reaction;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(03)01394-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Propionyl-coenzyme A synthetases (PrpE) of Salmonella choleraesuis and Ralstonia solanacearum sharing 62% identity in amino acid sequence to each other were cloned, expressed in Escherichia coli and purified. Both enzymes catalyzed acetyl-, propionyl-, butyryl- and acrylyl-coenzyme A formation with the highest k _cat/K _m values for propionate. They displayed sigmoidal homotrophic autoactivation kinetics for propionate but not for the other acyl substrates tested. Besides, substrate inhibition kinetics was observed for co-substrates, i.e. ATP and CoA. Based on the kinetic data reported herein, the reaction mechanisms of the enzyme are discussed.

【 授权许可】

Unknown