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The Substrate Specificity of Adenosine 3':5'-cyclic Monophosphate-dependent Protein Kinase of Rabbit Skeletal Muscle

Overview
Journal Biochem J
Specialty Biochemistry
Date 1977 Feb 15
PMID 192223
Citations 14
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Abstract

The known amino acid sequences at the two sites on phosphorylase kinase that are phosphorylated by cyclic AMP-dependent protein kinase were extended. The sequences of 42 amino acids around the phosphorylation site on the alpha-subunit and of 14 amino acids around the phosphorylation site on the beta-subunit were shown to be: alpha-subunit Phe-Arg-Arg-Leu-Ser(P)-Ile-Ser-Thr-Glu-Ser-Glx-Pro-Asx-Gly-Gly-His-Ser-Leu-Gly-Ala-Asp-Leu-Met-Ser-Pro-Ser-Phe-Leu-Ser-Pro-Gly-Thr-Ser-Val-Phe(Ser,Pro,Gly)His-Thr-Ser-Lys; beta-subunit, Ala-Arg-Thr-Lys-Arg-Ser-Gly-Ser(P)-VALIle-Tyr-Glu-Pro-Leu-Lys. The sites on histone H2B which are phosphorylated by cyclic AMP-dependent protein kinase in vitro were identified as serine-36 and serine-32. The amino acid sequence in this region is: Lys-Lys-Arg-Lys-Arg-Ser32(P)-Arg-Lys-Glu-Ser36(P)-Tyr-Ser-Val-Tyr-Val- [Iwai, K., Ishikawa, K. & Hayashi, H. (1970) Nature (London) 226, 1056-1058]. Serine-36 was phosphorylated at 50% of the rate at which the beta-subunit of phosphorylase kinase was phosphorylated, and it was phosphorylated 6-7-fold more rapidly than was serine-32. The amino acid sequences when compared with those at the phosphorylation sites of other physiological substrates suggest that the presence of two adjacent basic amino acids on the N-terminal side of the susceptible serine residue may be critical for specific substrate recognition in vivo.

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References
1.
Kemp B, Bylund D, Huang T, KREBS E . Substrate specificity of the cyclic AMP-dependent protein kinase. Proc Natl Acad Sci U S A. 1975; 72(9):3448-52. PMC: 433011. DOI: 10.1073/pnas.72.9.3448. View

2.
Edlund B, Andersson J, Titanji V, Dahlqvist U, Ekman P, ZETTERQVIST O . Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase. Biochem Biophys Res Commun. 1975; 67(4):1516-21. DOI: 10.1016/0006-291x(75)90198-9. View

3.
Yeaman S, Cohen P . The hormonal control of activity of skeletal muscle phosphorylase kinase. Phosphorylation of the enzyme at two sites in vivo in response to adrenalin. Eur J Biochem. 1975; 51(1):93-104. DOI: 10.1111/j.1432-1033.1975.tb03910.x. View

4.
Shlyapnikov S, Arutyunyan A, Kurochkin S, Memelova L, Nesterova M, Sashchenko L . Investigation of the sites phosphorylated in lysine-rich histones by protein kinase from pig brain. FEBS Lett. 1975; 53(3):316-9. DOI: 10.1016/0014-5793(75)80045-7. View

5.
Cohen P, Watson D, DIXON G . The hormonal control of activity of skeletal muscle phosphorylase kinase. Amino-acid sequences at the two sites of action of adenosine-3':5'-monophosphate-dependent protein kinase. Eur J Biochem. 1975; 51(1):79-92. DOI: 10.1111/j.1432-1033.1975.tb03909.x. View