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Cited by 198

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Substrate specificity of the cyclic AMP-dependent protein kinase.

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Kemp, B E, Bylund, D B, Huang, T S, Krebs, E G·1975·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Kemp, B. E., Bylund, D. B., Huang, T. S., & Krebs, E. G.
Venue
Proceedings of the National Academy of Sciences
Published
1975-09
Volume
72
Issue
9
Pages
3448-3452
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2030349770
Cited by
198
References
0
FWCI
4.42
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Substrate specificity of the cyclic AMP-dependent protein kinase. https://app.cochat.ai/papers/10.1073/pnas.72.9.3448
The paper
Kemp, B. E., Bylund, D. B., Huang, T. S., & Krebs, E. G. (1975). Substrate specificity of the cyclic AMP-dependent protein kinase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.72.9.3448

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.