Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate-protein ligase A

文献类型： 外文期刊

第一作者： Zhang, Xinyi

作者： Zhang, Xinyi;Nie, Jinglei;Zheng, Yuanmin;Ren, Jie;Zeng, An-Ping;Zeng, An-Ping;Ren, Jie

作者机构：

关键词： H protein; hydrolysis; lipoate-protein ligase A; lipoylation; protein interaction

期刊名称：BIOTECHNOLOGY AND BIOENGINEERING （ 影响因子：4.53； 五年影响因子：4.63 ）

ISSN： 0006-3592

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收录情况： SCI

摘要： Protein lipoylation is essential for the function of many key enzymes but barely studied kinetically. Here, the two-step reaction cascade of H protein lipoylation catalyzed by the multifunctional enzyme lipoate-protein ligase A (LplA) was quantitatively and differentially studied. We discovered new phenomena and unusual kinetics of the cascade: (a) the speed of the first reaction is faster than the second one by two orders of magnitude, leading to high accumulation of the intermediate lipoyl-AMP (Lip-AMP); (b) Lip-AMP is hydrolyzed, but only significantly at the presence of H protein and in competition with the lipoylation; (c) both the lipoylation of H protein and its hydrolysis is enhanced by the apo and lipoylated forms of H protein and a mutant without the lipoylation site. A conceptual mechanistic model is proposed to explain these experimental observations in which conformational change of LplA upon interaction with H protein and competitive nucleophilic attacks play key roles.

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