Wiesenfeld M, Schimpfessel L, Crokaert R
Biochim Biophys Acta. 1975 Oct 20;405(2):500-12. doi: 10.1016/0005-2795(75)90115-4.
Three forms of NAD-dependent alcohol dehydrogenase have been characterized in yeast by their heat sensitivity, their specificity and their electrophoretic patterns. Thermal stability increases in the following order: alcohol dehydrogenase I (fermentative enzyme), alcohol dehydrogenase II (oxidative enzyme), alcohol dehydrogenase III (mitochondrial enzyme). Work with isolated mitochondria shows that alcohol dehydrogenase III is the only form of alcohol dehydrogenase present in these organelles. Starch gel electrophoresis of alcohol dehydrogenase III reveals an active zone of slow migration which consists of five sub-bands. The relative activity of these five sub-bands varies with the conditions of growth. Mitochondrial alcohol dehydrogenase represents never more than 10% of the total cellular alcohol dehydrogenase. Information for its biosynthesis seems to be located in nucleic DNA. The mitochondrial enzyme shows a high affinity for alcohols with a double bond conjugated to the alcohol function.
通过热敏感性、特异性及电泳图谱，已在酵母中鉴定出三种形式的NAD依赖性乙醇脱氢酶。热稳定性按以下顺序增加：乙醇脱氢酶I（发酵酶）、乙醇脱氢酶II（氧化酶）、乙醇脱氢酶III（线粒体酶）。对分离线粒体的研究表明，乙醇脱氢酶III是这些细胞器中存在的唯一乙醇脱氢酶形式。乙醇脱氢酶III的淀粉凝胶电泳显示出一个迁移缓慢的活性区，它由五个亚带组成。这五个亚带的相对活性随生长条件而变化。线粒体乙醇脱氢酶占细胞总乙醇脱氢酶的比例从不超过10%。其生物合成信息似乎位于核DNA中。线粒体酶对具有与醇功能共轭双键的醇具有高亲和力。
