2 FUNCTIONALLY DIFFERENT DIHYDROOROTIC DEHYDROGENASES IN BACTERIA
2 FUNCTIONALLY DIFFERENT DIHYDROOROTIC DEHYDROGENASES IN BACTERIA
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DOI：
10.1128/jb.91.6.2251-2256.1966
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发表时间：
1966-01-01
影响因子：
3.2
通讯作者：
EAMES, DF
中科院分区：
文献类型：
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作者：
TAYLOR, WH;TAYLOR, ML;EAMES, DF
我们研究了细菌产生的两种二氢乳清酸脱氢酶之间的关系。从湖岸泥中分离到一种假单胞菌，能在以葡萄糖、天冬氨酸、甘油或乳清酸为碳源的盐培养基上生长。当碳源为乳清酸、葡萄糖、甘油或天冬氨酸时，假单胞菌形成了一种与颗粒结合的二氢乳清酸脱氢酶，类似于大肠杆菌中的生物合成酶。一个可溶性的，降解烟酰胺腺嘌呤二核苷酸磷酸连接的二氢乳清酸脱氢酶，以及颗粒结合的生物合成酶，形成时的假单胞菌乳清酸培养。生物合成酶与氧或铁氰化物连接，但不与吡啶核苷酸连接。当在葡萄糖上培养时，发酵杆菌只含有生物合成型的二氢乳清酸脱氢酶。根据以下观察结果，提出假单胞菌中存在两种功能不同的二氢乳清酸脱氢酶：两种酶的活性通过离心分离，只有当乳清酸存在于生长培养基中时，才形成吡啶核苷酸连接的活性;生物合成酶在[长划线]20 ℃下储存4个月是稳定的，而在这些条件下储存会破坏降解酶的活性。
We have investigated the relationship between the two kinds of dihydroorotic dehydrogenases produced by bacteria. A pseudomonad, capable of growth on a salts medium with glucose, aspartate, glycerol, or orotate as the carbon source, was isolated from lake bank mud. A particle-bound dihydroorotic dehydrogenase, similar to the biosynthetic enzyme in Escherichia coli, was formed by the pseudomonad when the carbon source was orotate, glucose, glycerol, or aspartate. A soluble, degradative nico-tinamide adenine dinucleotide phosphate-linked dihydrorotic dehydrogenase, as well as the particle-bound biosynthetic enzyme, was formed when the pseudomonad was cultivated on orotate. The biosynthesis enzyme links to oxygen or ferricyanide, but not to pyridine nucleotides. Zymobacterium oroticum, when cultivated on glucose, contained only the biosynthetic type of dihydrorotic dehydrogenase. The presence of two functionally different dihydroorotic dehydrogenases in the pseudomonad was suggested on the basis of the following observations: the two enzyme activities were separated by centrifugation; the pyridine nucleotide-linked activity was formed only when orotate was present in the growth medium; and the biosynthetic enzyme was stable to storage at [long dash]20 C for 4 months, whereas the degradative enzyme activity was destroyed by storage under these conditions.