Cytochrome P450BM-3 (CYP102): Regiospecificity of oxidation of .omega.-unsaturated fatty acids and mechanism-based inactivation
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00212a044
Reference40 articles.
1. Fatty acid monooxygenation by cytochrome P-450BM-3.
2. Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo- and flavoprotein domains.
3. Crystallization and preliminary x-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily.
4. Fatty acid monooxygenation by P450BM-3: Product identification and proposed mechanisms for the sequential hydroxylation reactions
5. The catalytic site of rat hepatic lauric acid omega-hydroxylase. Protein versus prosthetic heme alkylation in the omega-hydroxylation of acetylenic fatty acids.
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