Structural highlights
Publication Abstract from PubMed
Transesterification of fatty acids yields the essential component of biodiesel, but current processes are cost-prohibitive and generate waste. Recent efforts make use of biocatalysts that are effective in diverting products from primary metabolism to yield fatty acid methyl esters in bacteria. These biotransformations require the fatty acid O-methyltransferase (FAMT) from Mycobacterium marinum (MmFAMT). Although this activity was first reported in the literature in 1970, the FAMTs have yet to be biochemically characterized. Here, we describe several crystal structures of MmFAMT, which highlight an unexpected structural conservation with methyltransferases that are involved in plant natural product metabolism. The determinants for ligand recognition are analyzed by kinetic analysis of structure-based active-site variants. These studies reveal how an architectural fold employed in plant natural product biosynthesis is used in bacterial fatty acid O-methylation.
Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.,Petronikolou N, Nair SK Chem Biol. 2015 Nov 19;22(11):1480-90. doi: 10.1016/j.chembiol.2015.09.011. Epub , 2015 Oct 29. PMID:26526103[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Petronikolou N, Nair SK. Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel. Chem Biol. 2015 Nov 19;22(11):1480-90. doi: 10.1016/j.chembiol.2015.09.011. Epub , 2015 Oct 29. PMID:26526103 doi:http://dx.doi.org/10.1016/j.chembiol.2015.09.011
