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

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A novel Ca2+/calmodulin-dependent protein kinase lacking autophosphorylation activity in the rabbit heart.

We report the discovery, semi-purification and characterization of a novel Ca2+/calmodulin-dependent protein kinase (peak I kinase) using syntide 2 as a substrate from the rabbit heart. In the study of dependence of peak I kinase on the concentration of calmodulin, half-maximal activation was obtained at approx. 2.0 x 10(-7) M calmodulin. Peak I kinase did not undergo autophosphorylation. This kinase phosphorylates the synthetic peptides such as syntide 2, autocamtide-2, site 3 in a Ca2+/CaM-dependent manner, but not myosin light chain-peptide, gamma-peptide, and cAMP Response Element Binding Protein (CREB) peptide. Elongation Factor-2, alpha-casein and histone-IIIs were not phosphorylated. These data indicate that this CaM kinase is different from other identified Ca2+/calmodulin-dependent protein kinases and therefore constitutes a novel protein kinase.[1]

References

  1. A novel Ca2+/calmodulin-dependent protein kinase lacking autophosphorylation activity in the rabbit heart. Uemura, A., Okazaki, K., Takesue, H., Matsubara, T., Hidaka, H. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
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