Wang L, Kusaka T, Goldman D S
J Bacteriol. 1970 Mar;101(3):781-5. doi: 10.1128/jb.101.3.781-785.1970.
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.
结核分枝杆菌H37Ra菌株的无细胞提取物含有一种可溶性酶系统,该系统催化长链脂肪酸的延伸反应。主要反应涉及向受体脂肪酸添加单个C(2)单元;延伸仅在受体分子的羧基末端发生。内源性受体脂质可通过对酶系统进行溶剂萃取去除。脂质耗尽的酶可用外部酰基辅酶A完全重新激活,之后会发生与乙酰辅酶A的延伸反应。延伸反应对抗生物素蛋白不敏感,且不需要三磷酸腺苷。还原型烟酰胺腺嘌呤二核苷酸是还原当量的来源,而还原型烟酰胺腺嘌呤二核苷酸磷酸则无作用。