来自能够在1,2-丙二醇上生长的大肠杆菌突变体的亚铁激活烟酰胺腺嘌呤二核苷酸连接脱氢酶。
Ferrous-activated nicotinamide adenine dinucleotide-linked dehydrogenase from a mutant of Escherichia coli capable of growth on 1, 2-propanediol.
作者信息
Sridhara S, Wu T T, Chused T M, Lin E C
出版信息
J Bacteriol. 1969 Apr;98(1):87-95. doi: 10.1128/jb.98.1.87-95.1969.
Abstract
A nicotinamide adenine dinucleotide-linked dehydrogenase has been partially purified from a mutant of Escherichia coli K-12 able to grow on l-1,2-propanediol as carbon and energy source. This enzyme catalyzes the dehydrogenation at carbon 1 of l-1,2-propanediol, glycerol, 1,3-propanediol, ethylene glycol, and ethyl alcohol. The purified protein requires added ferrous or managanous ions. The V(max) and the apparent K(m) for a given substrate vary with the particular metal used.
摘要
一种烟酰胺腺嘌呤二核苷酸连接的脱氢酶已从大肠杆菌K-12的一个突变体中部分纯化出来，该突变体能够以l-1,2-丙二醇作为碳源和能源生长。这种酶催化l-1,2-丙二醇、甘油、1,3-丙二醇、乙二醇和乙醇在碳1位的脱氢反应。纯化后的蛋白质需要添加亚铁离子或锰离子。给定底物的V(max)和表观K(m)会因所使用的特定金属而有所不同。
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