DIOL DEHYDRATASE AND DIOL METABOLISM IN CLOSTRIDIUM GLYCOLICUM

乙二醇和丙烯发酵的代谢途径 研究了由Clostridium glycolicum产生的乙二醇，并研究了其水平。 测定了5种酶。 二醇脱氢酶，第一种酶 在该途径中，被发现是膜结合的，并且对 氧气 对该酶进行各种处理，以便 使其从基质中溶解。 只有有限的蛋白水解被发现， 从细胞膜上释放出少量的酶活性。 添加 已知影响钴酰胺辅酶活性的不同化合物 依赖性酶对二醇脱氢酶的活性没有影响， 提出了一种新的反应机理。 酶被强烈抑制 几种化合物，其中包括自由基清除剂， 和羟基脲。 结合EPR的初步实验 抑制实验表明，自由基可能参与 催化机理

The metabolic pathway of the fermentation of ethylene glycol and propylene glycol by Clostridium glycolicum was investigated and the levels of the five enzymes involved were determined. Diol dehydratase, the first enzyme in the pathway, was found to be membrane bound and very sensitive to oxygen. The enzyme was subjected to various treatments in order to solubilize it from its matrix. Only limited proteolysis was found to release small amounts of enzyme activity from the membrane. Addition of different compounds known to affect the activity of cobamide coenzyme dependent enzymes had no influence on the activity of diol dehydratase, suggesting a novel reaction mechanism. The enzyme was strongly inhibited by several compounds, among them radical scavengers such as hydroxylamine and hydroxyurea. Preliminary EPR experiments in combination with the inhibition experiment indicate the possible involvement of a radical in the catalytic mechanism.