Abstract
l-Xylulose reductase is part of the eukaryotic pathway for l-arabinose catabolism. A previously identified l-xylulose reductase in Hypocrea jecorina turned out to be not the 'true' one since it was not upregulated during growth on l-arabinose and the deletion strain showed no reduced l-xylulose reductase activity but instead lost the d-mannitol dehydrogenase activity [17]. In this communication we identified the 'true' l-xylulose reductase in Aspergillus niger. The gene, lxrA (JGI177736), is upregulated on l-arabinose and the deletion results in a strain lacking the NADPH-specific l-xylulose reductase activity and having reduced growth on l-arabinose. The purified enzyme had a Km for l-xylulose of 25mM and a νmax of 650U/mg.
| Original language | English |
|---|---|
| Pages (from-to) | 3540-3544 |
| Journal | FEBS Letters |
| Volume | 584 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - 1 Aug 2010 |
| MoE publication type | A1 Journal article-refereed |
Funding
This work was financially supported by the Academy of Finland through the research programme “White Biotechnology – Green Chemistry”, The Finnish Centre of Excellence Programme, 2008–2013, Project No. 118573 and an Academy Research Fellowship for P.R. We thank Anne Usvalampi for the l -xylulose producing E. coli strain.
Keywords
- Aspergillus niger
- EC 1.1.1.10
- L-Arabinose metabolism
- L-Xylulose
- Pentose
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