Elongation of fatty acids in Mycobacterium tuberculosis.
Cell-free extracts of the H37Ra strain of Mycobacterium tuberculosis contain a soluble enzyme system which catalyzes an elongation reaction of long-chain fatty acids. The predominant reaction involves the addition of a single C(2) unit to the acceptor fatty acid; the elongation takes place exclusively at the carboxyl end of the acceptor molecule. The endogenous acceptor lipid can be removed by solvent extraction of the enzyme system. The lipid-depleted enzyme can be fully reactivated with external acyl coenzyme A, after which elongation with acetyl coenzyme A takes place. The elongation reaction is avidin-insensitive and does not require adenosine triphosphate. Reduced nicotinamide adenine dinucleotide is the source of reducing equivalent, whereas reduced nicotinamide adenine dinucleotide phosphate is without effect.
D002247:Carbon Isotopes; D002849:Chromatography, Gas; D003065:Coenzyme A / Q000378:metabolism; D005227:Fatty Acids / Q000302:isolation & purification / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism
D002247:Carbon Isotopes; D005227:Fatty Acids; D009243:NAD; D009249:NADP; D003065:Coenzyme A