Flick P K, Bloch K
J Biol Chem. 1975 May 10;250(9):3348-51.
Palmitoyl-CoA dissociates the fatty acid synthetase complex from Mycobacterium smegmatis into inactive subunits of molecular weight 250,000 as determined by sucrose density gradient centrifugation. Palmitoyl-CoA binds to the subunits but the binding can be prevented and reversed by the mycobacterial 3-O-methylmannose-containing polysaccharide. When the palmitoyl-CoA containing inactive subunits were isolated by gel filtration on Sepharose 6B, and then concentrated and dialyzed against 0.5 M phosphate buffer, pH 7.0, containing 3 mM of the complexing agent heptakis-(2,6-di-O-methyl)-beta-cyclodextrin, activity was regenerated to the level of 40 percent of a control sample. The reversibility of the dissociation and inactivation of the synthetase by palmitoyl-CoA suggests that this end product might play a regulatory role by acting as a feedback inhibitor.
通过蔗糖密度梯度离心法测定，棕榈酰辅酶A可将耻垢分枝杆菌的脂肪酸合成酶复合物解离为分子量为250,000的无活性亚基。棕榈酰辅酶A与这些亚基结合，但分枝杆菌含3 - O - 甲基甘露糖的多糖可阻止并逆转这种结合。当通过Sepharose 6B凝胶过滤分离出含棕榈酰辅酶A的无活性亚基，然后浓缩并在含有3 mM络合剂七（2,6 - 二 - O - 甲基）-β - 环糊精的0.5 M pH 7.0磷酸盐缓冲液中透析时，活性恢复至对照样品水平的40%。棕榈酰辅酶A使合成酶解离和失活的可逆性表明，这种终产物可能作为反馈抑制剂发挥调节作用。
