Fatty acid monooxygenation by cytochrome P-450BM-3.

Coding nucleotide, 5' regulatory, and deduced amino acid sequences of P-450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium.

Cytochrome P-450BM-3 (P-450BM-3) from Bacillus megaterium incorporates both a P-450 and an NADPH:P-450 reductase in proteolytically separable domains of a single, 119-kDa polypeptide and functions as a fatty acid monooxygenase independently of any other protein. A 5-kilobase DNA fragment which contains the gene encoding P-450BM-3 was sequenced. A single continuous open reading frame starting at...

Cytochrome P-450 isoenzymes involved in fatty acid metabolism.

Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P-450-mediated hydroxylation.

In previous publications [English, Hughes and Wolf (1994) J. Biol. Chem. 269, 26836-26841; English, Hughes and Wolf (1996) Biochem. J. 316, 279-283], we have demonstrated that peroxisome proliferators and non-steroidal anti-inflammatory drugs are inducers of the cytochrome P-450BM-3 gene in Bacillus megaterium ATCC14581. Their mechanism of action involves binding to and subsequent displacement ...

Modulation of fatty acid signalling by cytochrome P-450-mediated hydroxylation.

Cockcroft, S., Thomas, G. M. H., Fensome, A., Geny, B., Cunningham, E., Gout, I., Hiles, I., Totty, N. F., Truong, 0. and Hsuan, J. J. (1994) Science 263,523-526 Martin, A., Brown, F. D., Hodgkin, M. N., Bradwell, A. J., Cook, S. J., Hart, M. and Wakelam, M. J. 0. (1996) J. Biol. Chem. 271, 17397-17403 Liscovitch, M., Chalifa, V., Pertiles, P., Chen, C. S. and Cantley, L. C. (1994) J. Biol. Che...

Drug and fatty acid hydroxylation by solubilized human liver microsomal cytochrome P-450-phospholipid requirement.

sideration in the literature [13]. As a result, the findings obtained in this investigation may be applicable to the study of PMA in other cell systems. According to Augustinsson [S], each esterase type exists in multiple forms and each animal species has its own typical spectrum of esterases in plasma and tissues [14]. In the presence of marked variations in location, form and activity, one mi...