Analysis of the phosphoryl transfer mechanism of c-AMP dependent protein kinase (PKA) by penta-coodinate phosphoric transition state theory

被引：9
作者：
Ni, F
Li, W
Li, YM
Zhao, YF [1 ]
机构：
[1] Xiamen Univ, Dept Chem, Key Lab Chem Biol Fujian Province, Xiamen 361005, Peoples R China
[2] Tsing Hua Univ, Sch Life Sci & Engn, Dept Chem, Key Lab Bioorgan Posphorus Chem, Beijing 100084, Peoples R China
来源：
CURRENT PROTEIN & PEPTIDE SCIENCE | 2005年 / 6卷 / 05期
关键词：
cAMP dependent protein kinase (PKA); phosphoryl; amino acid; penta-coodinate; phosphoric intermediate; hexacoodinate phosphoric intermediate; phosphoryl transfer mechanism; lysine participation;
D O I：
10.2174/138920305774329296
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
This review briefly covers recent literature of research on the phosphoryl transfer mechanism of PKA. Combining experimental and theoretical calculation results on enzymes with experimentally observed biomimic activities of phosphoryl amino acids and a small molecular model of catalytic core in PKA, a novel mechanism was proposed. The cooperative participation roles of both Asp166 and Lys168 via a penta-coodinate phosphoric intermediate was elucidated to conciliate the current different views of the phosphoryl transfer mechanism of PKA. Since many ATP-binding enzymes may share a similar phosphoryl transfer mechanism, this proposed mechanism might also apply to the mechanism of these enzymes, e.g., molecular motor and phosphatase among others.
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收藏
页码：437 / 442
页数：6
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