A cyclic AMP-independent protein kinase from Candida albicans.
A cyclic AMP-independent protein kinase which phosphorylates casein was purified to homogeneity from Candida albicans by affinity and ion-exchange chromatography. This protein kinase exhibits maximal activity with casein as substrate and is not stimulated by cyclic AMP or cyclic GMP. The Mr of the purified enzyme is 115,000, as determined by h.p.l.c. It migrates as a single band on gel electrophoresis and has three non-identical subunits, of Mr 44,000, 28,500 and 26,000, as determined by SDS/polyacrylamide-gel electrophoresis. This enzyme is insensitive to heparin, but is inhibited by polyamines. Furthermore, it is sensitive to thermal denaturation and to thiol reagents.
D002176:Candida albicans / Q000201:enzymology*; D002846:Chromatography, Affinity; D000242:Cyclic AMP / Q000494:pharmacology*; D006493:Heparin / Q000494:pharmacology; D008970:Molecular Weight; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology; D013379:Substrate Specificity
D047428:Protein Kinase Inhibitors; D013096:Spermine; D006493:Heparin; D000242:Cyclic AMP; D011494:Protein Kinases; D013095:Spermidine