PURIFICATION AND PROPERTIES OF GENTISATE 1,2-DIOXYGENASE FROM MORAXELLA-OSLOENSIS
PURIFICATION AND PROPERTIES OF GENTISATE 1,2-DIOXYGENASE FROM MORAXELLA-OSLOENSIS
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DOI：
10.1128/jb.121.3.794-799.1975
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发表时间：
1975-01-01
影响因子：
3.2
通讯作者：
CHAPMAN, PJ
中科院分区：
文献类型：
--
作者：
CRAWFORD, RL;HUTTON, SW;CHAPMAN, PJ
龙胆酸：将来自奥斯陆莫拉氏菌的氧1，2-氧化还原酶（脱环）（EC 1.13.11.4;龙胆酸1，2-双加氧酶）纯化至聚丙烯酰胺凝胶电泳所示的均一性。该酶的分子量约为154，000，在十二烷基硫酸钠存在下产生分子量为40，000的亚基。龙胆酸1，2-双加氧酶表现出广泛的底物特异性，并攻击一系列卤素和烷基取代的龙胆酸。马来酰丙酮酸，龙胆酸形成的产品，被细胞提取物补充还原型谷胱甘肽降解，但取代的马来酰丙酮酸酯在这些条件下不攻击。
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.