Configuration of the active Mg-ATP complex in protein kinase C reaction.
FEBS Lett
; 201(1): 94-6, 1986 May 26.
Article
em En
| MEDLINE
| ID: mdl-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.
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Base de dados:
MEDLINE
Assunto principal:
Proteína Quinase C
/
Trifosfato de Adenosina
Limite:
Animals
Idioma:
En
Ano de publicação:
1986
Tipo de documento:
Article