The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2

FEBS Lett. 1985 Jul 22;187(1):21-4. doi: 10.1016/0014-5793(85)81205-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Chromatography, High Pressure Liquid
  • Cyclic AMP / metabolism
  • Cytochrome P-450 Enzyme System / metabolism*
  • Isoenzymes / metabolism*
  • Microsomes, Liver / enzymology*
  • Phenobarbital / pharmacology
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Pseudomonas / enzymology
  • Rabbits
  • Rats
  • Serine / metabolism
  • Trypsin / metabolism


  • Amino Acids
  • Isoenzymes
  • Serine
  • Cytochrome P-450 Enzyme System
  • Cyclic AMP
  • Protein Kinases
  • Trypsin
  • Phenobarbital