ANAEROBIC OXIDATION OF DIHYDROOROTATE BY ESCHERICHIA-COLI K-12
ANAEROBIC OXIDATION OF DIHYDROOROTATE BY ESCHERICHIA-COLI K-12
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DOI：
10.1016/0005-2728(77)90197-9
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发表时间：
1977-01-01
期刊：
影响因子：
--
通讯作者：
GIBSON, F
中科院分区：
文献类型：
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作者：
ANDREWS, S;COX, GB;GIBSON, F
在厌氧条件下，使用各种突变的E. coli K-12。在葡萄糖基本培养基中厌氧生长的细胞中的这种氧化作用通过甲基萘醌与由frd基因编码的延胡索酸还原酶相联系，并且不依赖于细胞色素。相同的二氢乳清酸脱氢酶蛋白在二氢乳清酸的厌氧和有氧氧化中起作用。铁氰化物可以作为二氢乳清酸脱氢酶的人工电子受体，并且二氢乳清酸-甲萘醌-铁氰化物还原酶活性可以被2 M盐酸胍增溶而几乎没有活性损失。
The oxidation of dihydroorotate under anaerobic conditions was examined using various mutant strains of E. coli K-12. This oxidation in cells grown anaerobically in a glucose minimal medium is linked via menaquinone to the fumarate reductase enzyme coded for by the frd gene and is independent of the cytochromes. The same dihydroorotate dehydrogenase protein functions in the anaerobic and aerobic oxidation of dihydroorotate. Ferricyanide can act as an artificial electron acceptor for dihydroorotate dehydrogenase and the dihydroorotate-menaquinone-ferricyanide reductase activity can be solubilized by 2 M guanidine.cntdot.HCl with little loss of activity.