title: ω-versus(ω-1)-hydroxylation: Cytochrome P450 4B1 sterics make the call.
abstract: Many family 4 cytochrome P450s play key roles in fatty acid hydroxylation at the terminal, or ω, carbon, but the mechanistic basis for this energetically disfavored regiostereochemistry has been less clear. A co-crystal structure of the rabbit family 4 enzyme CYP4B1 with its substrate octane reveals that the propensity for ω-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond.
authors.affiliation: From the Departments of Medicinal Chemistry, Pharmacology, and Biophysics, University of Michigan, Ann Arbor, Michigan 48109 scottee@umich.edu.
authors.forename: Emily E
authors.initials: EE
authors.lastname: Scott
mesh_terms: D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005227:Fatty Acids / Q000378:metabolism; D006900:Hydroxylation; D009795:Octanes / Q000737:chemistry / Q000378:metabolism; D011817:Rabbits; D013379:Substrate Specificity
chemical_list: D005227:Fatty Acids; D009795:Octanes; D001189:Aryl Hydrocarbon Hydroxylases; C095029:cytochrome P-450 CYP4B1; C026728:octane