Kinetics of CheY phosphorylation by small molecule phosphodonors

FEBS Letters

Stock, Jeffry B.²  Da Re, Sandra S.²  Deville-Bonne, Dominique¹  Tolstykh, Tatiana²  Véron, Michel¹ 

[1] Unité de Régulation Enzymatique des Activités Cellulaires, CNRS URA 1773, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris, Cedex 15, France;Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA

关键词: Two-component system;    Phosphotransfer;    Chemotaxis;    AcP;    acetyl phosphate;    HPK;    histidine protein kinase;    Pam;    Phosphoramidate;   

DOI  :  10.1016/S0014-5793(99)01057-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor (K _s≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site.

【 授权许可】

Unknown