McKelvey J R, Fioravanti C F
Comp Biochem Physiol B. 1984;77(4):737-42. doi: 10.1016/0305-0491(84)90306-7.
Acetylpyridine NADP replaced NADP in promoting the Mn2+ ion-requiring mitochondrial "malic" enzyme of Hymenolepis diminuta. Disrupted mitochondria displayed low levels of an apparent oxaloacetate-forming malate dehydrogenase activity when NAD or acetylpyridine NAD served as the coenzyme. Significant malate-dependent reduction of acetylpyridine NAD by H. diminuta mitochondria required Mn2+ ion and NADP, thereby indicating the tandem operation of "malic" enzyme and NADPH:NAD transhydrogenase. Incubation of mitochondrial preparations with oxaloacetate resulted in a non-enzymatic decarboxylation reaction. Coupling of malate oxidation with electron transport via the "malic" enzyme and transhydrogenase was demonstrated by polarographic assessment of mitochondrial reduced pyridine nucleotide oxidase activity.
在促进微小膜壳绦虫的需锰离子线粒体“苹果酸”酶方面,乙酰吡啶NADP取代了NADP。当NAD或乙酰吡啶NAD作为辅酶时,破碎的线粒体表现出低水平的明显形成草酰乙酸的苹果酸脱氢酶活性。微小膜壳绦虫线粒体对乙酰吡啶NAD的显著苹果酸依赖性还原需要锰离子和NADP,从而表明“苹果酸”酶和NADPH:NAD转氢酶的串联运作。用草酰乙酸孵育线粒体制剂会导致非酶促脱羧反应。通过对线粒体还原吡啶核苷酸氧化酶活性的极谱评估,证明了苹果酸氧化与通过“苹果酸”酶和转氢酶的电子传递的偶联。