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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Configuration of the active Mg-ATP complex in protein kinase C reaction. Kondo, H., Kinoshita, J., Matsuba, T., Sunamoto, J. FEBS Lett. (1986) [Pubmed]
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