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.