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. 1975 Sep;72(9):3448–3452. doi: 10.1073/pnas.72.9.3448

Substrate specificity of the cyclic AMP-dependent protein kinase.

B E Kemp, D B Bylund, T S Huang, E G Krebs
PMCID: PMC433011  PMID: 1059131

Abstract

The protein substrate specificity of the catalytic subunit of rabbit skeletal muscle cyclic AMP-dependent protein kinase (EC 2.7.1.37; ATP:protein phosphotransferase) has been studied using genetic variants of beta casein. It was found that beta casein-B was phosphorylated at a much greater rate than beta caseins A1, A2, A3, or C. The enhanced phosphorylation of beta casein-B, as compared with the most common variant A2, was attributed to an arginine substitution for a serine at position 122, which caused a nearby residue, serine 124, to become a phosphorylation site for the protein kinase. These results further support the concept that the local primary structure is important in specificity and that arginine may be a specific determinant common to all the local phosphorylation site sequences recognized by the cyclic AMP-dependent protein kinase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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