Chen Y M, Zhu Y, Lin E C
J Bacteriol. 1987 Jul;169(7):3289-94. doi: 10.1128/jb.169.7.3289-3294.1987.
Mutant analysis revealed that complete utilization of L-fucose and L-rhamnose by Escherichia coli requires the activity of a common NAD-linked aldehyde dehydrogenase which converts L-lactaldehyde to L-lactate. Mutations affecting this activity mapped to the ald locus at min 31, well apart from the fuc genes (min 60) encoding the trunk pathway for L-fucose dissimilation (as well as L-1,2-propanediol oxidoreductase) and the rha genes (min 88) encoding the trunk pathway for L-rhamnose dissimilation. Mutants that grow on L-1,2-propanediol as a carbon and energy source also depend on the ald gene product for the conversion of L-lactaldehyde to L-lactate.
突变分析表明,大肠杆菌对L-岩藻糖和L-鼠李糖的完全利用需要一种常见的NAD连接的醛脱氢酶的活性,该酶将L-乳醛转化为L-乳酸。影响该活性的突变定位于31分钟处的ald位点,与编码L-岩藻糖异化主干途径(以及L-1,2-丙二醇氧化还原酶)的fuc基因(60分钟处)和编码L-鼠李糖异化主干途径的rha基因(88分钟处)相距甚远。以L-1,2-丙二醇作为碳源和能源生长的突变体也依赖ald基因产物将L-乳醛转化为L-乳酸。