Dataset Information


The substrate specificity of adenosine 3':5'-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle.

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.


PROVIDER: S-EPMC1164615 | BioStudies | 1977-01-01

SECONDARY ACCESSION(S): 10.1042/bj1620411

REPOSITORIES: biostudies

Similar Datasets

1983-01-01 | S-EPMC1152171 | BioStudies
1991-01-01 | S-EPMC1151174 | BioStudies
1968-01-01 | S-EPMC1187117 | BioStudies
1989-01-01 | S-EPMC1135608 | BioStudies
1996-01-01 | S-EPMC1216895 | BioStudies
1989-01-01 | S-EPMC1138344 | BioStudies
1967-01-01 | S-EPMC1271246 | BioStudies
1978-01-01 | S-EPMC1184184 | BioStudies
1987-01-01 | S-EPMC1148042 | BioStudies
1000-01-01 | S-EPMC48192 | BioStudies