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首页> 外文期刊>Applied biochemistry and biotechnology, Part A. enzyme engineering and biotechnology >The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate
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The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate

机译:大肠杆菌的yjN编码L-半乳糖酸脱氢酶,可用于定量L-半乳糖酸和L-古洛糖酸

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摘要

Escherichia coli is able to utilize L-galactonate as a sole carbon source. A metabolic pathway for L-galactonate catabolism is described in E. coli, and it is known to be interconnected with D-galacturonate metabolism. The corresponding gene encoding the first enzyme in the L-galactonate pathway, L-galactonate-5-dehydrogenase, was suggested to be yjjN. However, L-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an L-galactonate dehydrogenase having activity also for L-gulonate. The K_m and k_(cat) for L-galactonate were 19.5±0.6 mM and 0.51±0.03 s~(-1), respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for L-galactonate and L-gulonate were 1.65 and 10 μM, respectively.
机译:大肠杆菌能够将L-半乳糖酸酯用作唯一的碳源。在大肠杆菌中描述了L-半乳糖酸酯分解代谢的代谢途径,并且已知其与D-半乳糖醛酸酯代谢相关。相应的编码L-半乳糖酸途径中第一个酶的基因,即L-半乳糖酸-5-脱氢酶,被称为yjjN。但是,从未用yjjN基因产物证明L-半乳糖酸脱氢酶活性。在这里,我们显示YjjN确实是具有对L-古洛糖酸的活性的L-半乳糖酸脱氢酶。 L-半乳糖酸酯的K_m和k_(cat)分别为19.5±0.6 mM和0.51±0.03 s〜(-1)。此外,YjjN还用于在耦合分析中对这两种物质进行定量检测。 L-半乳糖酸酯和L-古洛糖酸酯的检出限分别为1.65和10μM。

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