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

作者信息

Kondo H, Kinoshita J, Matsuba T, Sunamoto J

出版信息

FEBS Lett. 1986 May 26;201(1):94-6. doi: 10.1016/0014-5793(86)80576-2.

DOI:10.1016/0014-5793(86)80576-2
PMID:3486784
Abstract

To probe the active site structure of protein kinase C stereochemical studies were carried out by using ATP beta S. The enzyme utilizes either one of the diastereomers (SP and RP) of ATP beta S 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.

摘要

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