Structural highlights
Function
[CPXB_BACME] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
Publication Abstract from PubMed
Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450BM3 gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state FeIII-to-FeII reduction potential and substantially improves NAD(P)H-driven activity.
A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.,Coelho PS, Wang ZJ, Ener ME, Baril SA, Kannan A, Arnold FH, Brustad EM Nat Chem Biol. 2013 Jun 23. doi: 10.1038/nchembio.1278. PMID:23792734[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Coelho PS, Wang ZJ, Ener ME, Baril SA, Kannan A, Arnold FH, Brustad EM. A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat Chem Biol. 2013 Jun 23. doi: 10.1038/nchembio.1278. PMID:23792734 doi:10.1038/nchembio.1278
