Primary structure of the site on bovine hormone-sensitive lipase phosphorylated by cyclic AMP-dependent protein kinase.
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.
Garton
A J
AJ
Department of Biochemistry, University of Newcastle, Newcastle upon Tyne, England.
Campbell
D G
DG
Cohen
P
P
Yeaman
S J
SJ
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
D011494:Protein Kinases; D002787:Sterol Esterase; D014357:Trypsin