DIOL DEHYDRATASE AND DIOL METABOLISM IN CLOSTRIDIUM GLYCOLICUM

乙二醇和丙烯发酵的代谢途径 对甘氨酸梭菌产乙二醇菌进行了调查，并测定了菌体中 对所涉及的五种酶进行了测定。第一种酶--二醇脱水酶 在该途径中，被发现是膜结合的，对 氧气。该酶受到不同的处理，以便 从它的基质中溶解它。只有有限的蛋白质分解被发现 从膜上释放少量的酶活性。添加 已知的影响钴酰胺辅酶活性的不同化合物 依赖酶对二醇脱水酶的活性没有影响， 提出了一种新的反应机理。这种酶受到强烈的抑制 几种化合物，其中包括自由基清除剂，如羟胺 和羟基脲。初步的EPR实验结合 抑制实验表明，自由基可能参与了 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.