title: Cytochrome P-450-dependent fatty acid hydroxylase system in Japanese house musk shrew, Suncus murinus.
abstract: The substrate specificity and other properties of a fatty acid hydroxylase system in liver microsomes of the Japanese house musk shrew, Suncus murinus, were examined. Shrew liver microsomes catalyzed the hydroxylation of various saturated fatty acids (C8-C18) to the corresponding omega- and (omega-1)-hydroxy derivatives. The relative activities of the hydroxylase with these substrates were as follows: C12 (100, actual conversion: 7.05 nmol/mg of microsomal protein/min), C10 (90), C14 (87), C16 (23), C8 (19), and C18 (11). The specific activity of the fatty acid hydroxylase in shrew liver was much higher than that in other species. The omega/omega-1-hydroxylation ratio decreased with increasing chain length of fatty acid substrates (C10-C18), but it was 0 for the C8 fatty acid. Both NADPH and O2 were required for hydroxylase activity, and NADH had little effect. The apparent Km value for laurate was 1.6 X 10(-5) M. The hydroxylase activity was 92% inhibited by CO at a CO-O2 ratio of 9. p-Chloromercuribenzoate (0.1 mM) inhibited hydroxylation by 94% whereas iodoacetate (0.1 mM) inhibited it by only 8%. SKF 525-A (1 mM) and menadione (0.01 mM), respectively, caused 41% and 29% inhibition of the activity. It is concluded that the hydroxylase catalyzing fatty acid hydroxylation in shrew liver microsomes is a typical cytochrome P-450-linked monooxygenase.
mesh_terms: D000818:Animals; D042926:Cytochrome P-450 CYP4A; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004579:Electron Transport; D006900:Hydroxylation; D007564:Japan; D007700:Kinetics; D007848:Laurates / Q000378:metabolism; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D012788:Shrews / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D007848:Laurates; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D042926:Cytochrome P-450 CYP4A