The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2.
作者信息
Müller R, Schmidt W E, Stier A
出版信息
FEBS Lett. 1985 Jul 22;187(1):21-4. doi: 10.1016/0014-5793(85)81205-9.
PMID:2991008
Abstract
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.
摘要
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