title: Biochemical characterization of an S-adenosyl-l-methionine-dependent methyltransferase (Rv0469) of Mycobacterium tuberculosis.
abstract: Tuberculostearic acid (l0-methylstearic acid, TSA) is a major constituent of mycobacterial membrane phospholipids, and its biosynthesis involves the direct methylation of oleic acid esterified as a component of phospholipids. The methyltransferases of mycobacteria were long proposed to be involved in the synthesis of methyl-branched short-chain fatty acids, but direct experimental evidence is still lacking. In this study, we identified the methyltransferase encoded by umaA in Mycobacterium tuberculosis H37Rv as a novel S-adenosyl-l-methionine (SAM)-dependent methyltransferase capable of catalyzing the conversion of olefinic double bond of phospholipid-linked oleic acid to biologically essential TSA. Therefore, UmaA, catalyzing such modifications, offer a viable target for chemotherapeutic intervention.
authors: CSIR-Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Mall Road, Delhi 110007, India. meena@igib.res.in
authors: Laxman S
authors: LS
authors: Meena
authors: Puneet
authors: P
authors: Chopra
authors: Ram A
authors: RA
authors: Vishwakarma
authors: Yogendra
authors: Y
authors: Singh
mesh_terms: D003001:Cloning, Molecular; D005232:Fatty Acids, Volatile / Q000096:biosynthesis; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000378:metabolism*; D013229:Stearic Acids / Q000378:metabolism*
chemical_list: D005232:Fatty Acids, Volatile; D013229:Stearic Acids; C026082:tuberculostearic acid; D012436:S-Adenosylmethionine; D008780:Methyltransferases