Bar-Tana J, Rose G, Shapiro B
Biochem J. 1972 Oct;129(5):1101-7. doi: 10.1042/bj1291101.
The partial and exchange reactions of long-chain fatty acid activation were determined by using purified microsomal long-chain fatty acyl-CoA synthetase (EC 6.2.1.3). No significant ATP formation from palmitoyl-AMP and PP(i), nor palmitoyl-AMP-dependent CoA disappearance could be demonstrated. Similarly, no palmitate-dependent [(32)P(2)]PP(i)-ATP exchange was catalysed by the pure enzyme. The above partial and exchange reactions were, however, catalysed by the parent microsomal fraction at a rate similar to that of the overall reaction. The implications of these results are discussed.
通过使用纯化的微粒体长链脂肪酰辅酶A合成酶(EC 6.2.1.3)来测定长链脂肪酸活化的部分反应和交换反应。未证实棕榈酰-AMP和焦磷酸(PP(i))能显著形成ATP,也未证实棕榈酰-AMP依赖性辅酶A的消失。同样,纯酶也未催化棕榈酸依赖性的[(32)P(2)]PP(i)-ATP交换反应。然而,上述部分反应和交换反应可由微粒体母液以与总反应相似的速率催化。讨论了这些结果的意义。