奥斯陆莫拉菌中龙胆酸盐1,2-双加氧酶的纯化及性质
Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis.
作者信息
Crawford R L, Hutton S W, Chapman P J
出版信息
J Bacteriol. 1975 Mar;121(3):794-9. doi: 10.1128/jb.121.3.794-799.1975.
Abstract
Gentisate:oxygen 1,2-oxidoreductase (decyclizing) (EC 1.13.11.4; gentisate 1,2-dioxygenase) from Moraxella osloensis was purified to homogeneity as shown by polyacrylamide gel electrophoresis. The enzyme has a molecular weight of about 154,000 and gives rise to subunits of molecular weight 40,000 in the presence of sodium dodecyl sulfate. Gentisate 1,2-dioxygenase showed broad substrate specificity and attacked a range of halogen- and alkyl-substituted gentisic acids. Maleylpyruvate, the product formed from gentisate, was degraded by cell extracts supplemented with reduced glutathione, but substituted maleylpyruvates were not attacked under these conditions.
摘要
来自奥斯陆莫拉菌的龙胆酸盐
氧1,2-氧化还原酶（环化）（EC 1.13.11.4；龙胆酸盐1,2-双加氧酶）经聚丙烯酰胺凝胶电泳显示已纯化至同质。该酶的分子量约为154,000，在十二烷基硫酸钠存在下会产生分子量为40,000的亚基。龙胆酸盐1,2-双加氧酶表现出广泛的底物特异性，能作用于一系列卤素和烷基取代的龙胆酸。由龙胆酸盐形成的产物马来酰丙酮酸可被补充了还原型谷胱甘肽的细胞提取物降解，但在这些条件下，取代的马来酰丙酮酸不会被作用。
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