Configuration of the active Mg‐ATP complex in protein kinase C reaction

FEBS Letters

Matsuba, Takao¹  Sunamoto, Junzo¹  Kinoshita, Junko¹  Kondo, Hiroki¹ 

[1] Laboratory of Bioorganic Chemistry, Department of Industrial Chemistry, Nagasaki University, Nagasaki 852, Japan

关键词: Phosphorylation;    Protein kinase C;    ATPβS;    Stereospecificity;   

DOI  :  10.1016/0014-5793(86)80576-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To probe the active site structure of protein kinase C stereochemical studies were carried out by using ATPβs. The enzyme utilizes either one of the diastereomers (S_p and R_p ) of ATPβs almost equally well as a substrate. This result contrasts with that for cyclic AMP-dependent protein kinase, suggesting that the topography of the nucleotide-binding site is significantly different between the two kinases.

【 授权许可】

Unknown