The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2.
The phenobarbital-inducible form of cytochrome P-450 purified from rabbit liver microsomes is phosphorylated by cAMP-dependent protein kinase at a single site, the serine residue in position 128 of the amino acid sequence. The serine is located in a characteristic recognition sequence for cAMP-dependent protein kinase and is part of a primary structure which is conserved during evolution, present also in phenobarbital-inducible rat cytochrome and cytochrome P-450 CAM from Pseudomonas putida. The contribution of these findings to our understanding of the structure and membrane topology of cytochrome P-450 LM2 and its turnover regulated by phosphorylation is discussed.
Müller
R
R
Schmidt
W E
WE
Stier
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D000242:Cyclic AMP / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology*; D010634:Phenobarbital / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D012694:Serine / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D007527:Isoenzymes; D012694:Serine; D003577:Cytochrome P-450 Enzyme System; D000242:Cyclic AMP; D011494:Protein Kinases; D014357:Trypsin; D010634:Phenobarbital