Phosphorylation of microsome-bound cytochrome P-450 LM2.
The phosphorylation of a microsomal protein of rabbit liver by catalytic subunit of cyclic AMP-dependent protein kinase was shown, and the protein was identified as cytochrome P-450 LM2 on basis of comparative peptide-mapping. Acid hydrolysis of microsome-bound phosphorylated cytochrome P-450 revealed that phosphorylation occurred exclusively on serine residues. This serine residue was identified as the same residue phosphorylated in purified, soluble P-450, that is, serine in position 128.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D011817:Rabbits
D008565:Membrane Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D010768:Phosphoserine; D003577:Cytochrome P-450 Enzyme System