Phosphorylation of glycerol by cAMP-dependent protein kinase: comparison with src kinase.
The tyrosine-specific src kinase and the catalytic subunit of bovine heart adenosine 3',5'-cyclic monophosphate-dependent protein kinase phosphorylated glycerol when incubated with [gamma-32P]Mg-ATP. The product was detected by thin layer chromatography. The formation of glycerol phosphate by both enzymes was independent of the presence of a protein substrate (casein). The results show that glycerol phosphorylation is not a unique property of the src transforming protein. Because the product was only detected when high glycerol concentrations (approximately 0.1 M) were used, it is unlikely that either enzyme functions as a glycerol kinase in vivo.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000201:enzymology*; D002364:Caseins / Q000378:metabolism; D002384:Catalysis; D002417:Cattle; D002478:Cells, Cultured; D002855:Chromatography, Thin Layer; D003956:Dialysis; D005990:Glycerol / Q000378:metabolism*; D066298:In Vitro Techniques; D009206:Myocardium / Q000201:enzymology; D009374:Neoplasms, Experimental / Q000201:enzymology; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D002364:Caseins; D011494:Protein Kinases; D005990:Glycerol