title: Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA; Institute for Genomic Biology, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
authors.forename: Nektaria
authors.initials: N
authors.lastname: Petronikolou
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA; Center for Biophysics and Computational Biology and University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Roger Adams Lab Room 430, Urbana, IL 61801, USA; Institute for Genomic Biology, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. Electronic address: snair@illinois.edu.
authors.forename: Satish K
authors.initials: SK
authors.lastname: Nair
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D055162:Biocatalysis; D056804:Biofuels; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005227:Fatty Acids / Q000378:metabolism; D007700:Kinetics; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019910:Mycobacterium marinum / Q000201:enzymology*; D012435:S-Adenosylhomocysteine / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D056804:Biofuels; D005227:Fatty Acids; D012436:S-Adenosylmethionine; D012435:S-Adenosylhomocysteine; D008780:Methyltransferases; C070107:fatty acid methyltransferase