Kinetics of CheY phosphorylation by small molecule phosphodonors

Kinetics of CheY phosphorylation by small molecule phosphodonors
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DOI:
10.1016/s0014-5793(99)01057-1
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发表时间:
1999-09-03
期刊:
影响因子:
3.5
通讯作者:
Stock, JB
Stock, JB
中科院分区:
生物学3区
文献类型:
--
作者:
Da Re, SS;Deville-Bonne, D;Stock, JB

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趋化反应调节剂 CheY 可以从其相关的自磷酸化蛋白激酶 CheA 或小磷酸供体分子(例如乙酰磷酸)获得磷酰基。我们报告了乙酰磷酸对 CheY 磷酸化的停流动力学分析,结果表明 CheY 对这种磷酸供体具有非常低的亲和力(K-s,远大于 0.1 M), 与以下结论一致:虽然 CheY 为磷酸转移反应提供催化功能,但 CheA 激酶可能只是增加 CheY 活性位点的有效磷酸供体浓度。 (C) 1999 年欧洲生化学会联合会。
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, much greater than 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. (C) 1999 Federation of European Biochemical Societies.