Noy N, Zakim D
Biochim Biophys Acta. 1985 Feb 8;833(2):239-44. doi: 10.1016/0005-2760(85)90196-1.
The substrate specificity of fatty-acyl-CoA ligase in liver microsomes has been studied in a system in which fatty acids are present initially as complexes with unilamellar vesicles of phosphatidylcholine. The latter were prepared by cosonication of phospholipids and different fatty acids. As compared with previous studies of the enzyme the activity of acyl-CoA ligase is several-fold higher for assays carried out with fatty acid substrates added as components of a bilayer. This was true for all fatty acids studied. Also as compared with data reported previously in the literature there was a systematic relationship between the structure of fatty acids, activity at Vmax for synthesis of acyl-CoA and avidity of binding to the ligase. Activity at Vmax was greatest for lauric acid and decreased with increasing chain length. The apparent avidity of enzyme for fatty acids was greatest for octanoic acid and decreased as chain length increased.
在一个系统中，对肝脏微粒体中脂肪酰辅酶A连接酶的底物特异性进行了研究，在该系统中，脂肪酸最初以与磷脂酰胆碱单层囊泡形成的复合物形式存在。后者通过磷脂和不同脂肪酸的共超声处理制备。与该酶先前的研究相比，对于作为双层成分添加的脂肪酸底物进行的测定，酰基辅酶A连接酶的活性高出几倍。对所有研究的脂肪酸都是如此。同样与文献中先前报道的数据相比，脂肪酸的结构、酰基辅酶A合成的Vmax活性和与连接酶的结合亲和力之间存在系统关系。月桂酸的Vmax活性最高，并且随着链长增加而降低。酶对脂肪酸的表观亲和力对辛酸最高，并且随着链长增加而降低。
