title: Primary structure of the site on bovine hormone-sensitive lipase phosphorylated by cyclic AMP-dependent protein kinase.
abstract: The primary structure of a region on hormone-sensitive lipase was determined to be: Lys-Thr-Glu-Pro-Met-Arg-Arg-Ser- Val-Ser-Glu-Ala-Ala-Leu-Thr-Gln-Pro-Glu-Gly-Pro-Leu-Gly-Thr-Asp-Ser-Leu-Lys. Ser-8 was the only residue in the intact protein phosphorylated by cyclic AMP-dependent protein kinase. However, Ser-10 also appeared to be present in a phosphorylated form, suggesting that it is a target for a distinct protein kinase in vivo.
authors.affiliation: Department of Biochemistry, University of Newcastle, Newcastle upon Tyne, England.
authors.forename: A J
authors.initials: AJ
authors.lastname: Garton
authors.forename: D G
authors.initials: DG
authors.lastname: Campbell
authors.forename: P
authors.initials: P
authors.lastname: Cohen
authors.forename: S J
authors.initials: SJ
authors.lastname: Yeaman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D002787:Sterol Esterase / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
chemical_list: D011494:Protein Kinases; D002787:Sterol Esterase; D014357:Trypsin