Substrate specificity of the cyclic AMP-dependent protein kinase. | Zendy

Bruce E. Kemp | Zendy; Dan Bylund | Zendy; TzeSing Huang | Zendy; E G Krebs | Zendy

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Substrate specificity of the cyclic AMP-dependent protein kinase.

Author(s) -

Bruce E. Kemp,

Dan Bylund,

TzeSing Huang,

E G Krebs

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.9.3448

Subject(s) - casein kinase 2 , phosphotransferase , phosphorylation , protein kinase a , casein kinase 2, alpha 1 , biochemistry , serine , protein subunit , casein kinase 1 , biology , protein phosphorylation , cgmp dependent protein kinase , chemistry , cyclin dependent kinase 2 , gene

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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