Abstract
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 Km and kcat 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.
Original language | English |
---|---|
Pages (from-to) | 1829-1835 |
Number of pages | 7 |
Journal | Applied Biochemistry and Biotechnology |
Volume | 173 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2014 |
MoE publication type | A1 Journal article-refereed |
Keywords
- YjjN
- l-galactonate-5-dehydrogenase
- l-galactonate
- l-gulonate
- d-galacturonate
- E.coli