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Configuration of the active Mg‐ATP complex in protein kinase C reaction
Author(s) -
Kondo Hiroki,
Kinoshita Junko,
Matsuba Takao,
Sunamoto Junzo
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80576-2
Subject(s) - chemistry , microbiology and biotechnology , biochemistry , biology
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.