de Mata Z S, deBruyn B, Saz H J
Department of Biological Sciences, University of Notre Dame, IN 46556, USA.
Comp Biochem Physiol B Biochem Mol Biol. 1997 Mar;116(3):379-83. doi: 10.1016/s0305-0491(96)00266-0.
Acyl-CoA compounds are stable in adult Ascaris suum mitochondrial preparations. However, when incubated in the presence of 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB), acetyl-CoA or propionyl-CoA are hydrolyzed to form free coenzyme A. This acetyl-CoA hydrolase activity has been partially purified and found to be specific for the above CoA derivatives. Gel filtration indicates an apparent molecular weight of 232,000. The hydrolase activity has been purified free from acyl-CoA transferase activities and appears not to be accounted for on the basis of a thiolase. Because Ascaris is an intestinal parasite that metabolizes primarily anaerobically and accumulates a large number of volatile fatty acids that are formed as the coenzyme A derivatives, the hydrolase would be expected to function in the regeneration of free CoA. However, how the hydrolase reaction would be pulled in the absence of the nonphysiologic DTNB is not known.
酰基辅酶A化合物在成年猪蛔虫线粒体制剂中是稳定的。然而，当在5,5'-二硫代双（2-硝基苯甲酸）（DTNB）存在下孵育时，乙酰辅酶A或丙酰辅酶A会被水解形成游离辅酶A。这种乙酰辅酶A水解酶活性已被部分纯化，并且发现对上述辅酶A衍生物具有特异性。凝胶过滤表明其表观分子量为232,000。该水解酶活性已被纯化至不含酰基辅酶A转移酶活性，并且似乎不能用硫解酶来解释。由于蛔虫是一种主要进行无氧代谢的肠道寄生虫，并积累了大量作为辅酶A衍生物形成的挥发性脂肪酸，因此预计该水解酶在游离辅酶A的再生中起作用。然而，在没有非生理性DTNB的情况下，水解酶反应将如何进行尚不清楚。
