Chemical modification of microsomal cytochrome P450: role of lysyl residues in hydroxylation activity

FEBS Letters

Kunz, Barbara C.¹  Richter, Christoph¹ 

[1] Eidgenössische Technische Hochschule, Laboratorium für Biochemie I, Univresitätstrasse 16, CH-8092 Zürich, Switzerland

关键词: Microsomal monoxygenase;    Cytochrome P450 activity;    Acetylation;    Reconstitution;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PS;    phosphatidylserine;    SDS—PAGE;    sodium dodecylsulfate—polyacrylamide gel electrophoresis;    EDTA;    ethylene diaminetetraacetate;    HEPES;    4-(2-hydroxyethyl)-1-piperazineethane sulfonic acid;   

DOI  :  10.1016/0014-5793(83)81031-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cytochrome P450 purified from phenobarbital-induced rat liver microsomes was acetylated at 3 lysyl residues. When reconstituted with purified NADPH-cytochrome P450 reductase, the modified cytochrome showed full activity and substrate-induced spectral changes with d-benzphetamine. With 7-ethoxycoumarin, neither enzymic activity nor binding was detected. It is concluded that the positively charged lysine residues of cytochrome P450 are important for metabolism of 7-ethoxycoumarin by cytochrome P450.

【 授权许可】

Unknown