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The site of cyclic AMP‐dependent protein kinase catalyzed phosphorylation of cytochrome P‐450 LM2
Author(s) -
Müller R.,
Schmidt W.E.,
Stier A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81205-9
Subject(s) - cytochrome , phosphorylation , serine , biochemistry , protein kinase a , biology , chemistry , microbiology and biotechnology , enzyme
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 phenobarbitalinducible 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.