[Regulation of the catalytic activity of the monooxygenase enzyme system depending of the substrate structure and phospholipid composition of the model membrane].
A comparative study of pentoxy- and benzyloxyresorufin dealkylation by a monooxygenase enzyme system in dilauroylphosphatidylcholine micelles and in proteoliposomes was carried out. In proteoliposomes whose lipid matrix is formed by double phospholipid mixtures, a cooperative regulation of the oxidation reaction was found. It was shown that the cooperativity of this process depends on the substrate type as well as on the phospholipid composition of the vesicles and decreases during peroxide oxidation of lipids. The results obtained are discussed in terms of protein-protein and protein-phospholipid interactions in the oligomer ensembles consisting of several cytochrome P-450 LM2 molecules.
Kiselev
P A
PA
Garda
G
G
Finch
S A
SA
Stir
A
A
Khatyleva
S Iu
SIu
Akhrem
A A
AA
D000818:Animals; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D015227:Lipid Peroxidation; D008099:Liver / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids / Q000737:chemistry*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010743:Phospholipids / Q000737:chemistry*; D011510:Proteolipids; D011817:Rabbits; D013379:Substrate Specificity
D008563:Membrane Lipids; D010743:Phospholipids; D011510:Proteolipids; C020485:proteoliposomes; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases
Reguliatsiia kataliticheskoĭ aktivnosti monooksigenaznoĭ fermentoĭ sistemy v zavisimosti ot struktury substrata i fosfolipidnogo sostava model'noĭ membrany.