ArticleBiochemistry2013
A novel L-xylulose reductase essential for L-arabinose catabolism in Trichoderma reesei.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- L-arabinose: a strategic modulator of pathogen virulence for food system safety.Archives of microbiology · 2026Review
- Metabolic engineering of Saccharomyces cerevisiae for efficient utilization of pectin-rich biomass.Journal of microbiology (Seoul, Korea) · 2025Review
- Metabolomics distinguishes different grades ofHeliyon · 2024Article
- Non-canonical D-xylose and L-arabinose metabolism via D-arabitol in the oleaginous yeast Rhodosporidium toruloides.Microbial cell factories · 2023Article
- Characterization of a xylitol dehydrogenase fromFrontiers in bioengineering and biotechnology · 2022Article
- Engineering microbial pathways for production of bio-based chemicals from lignocellulosic sugars: current status and perspectives.Biotechnology for biofuels · 2020Review
- The gold-standard genome ofStudies in mycology · 2018Article
- Understanding Functional Roles of Native Pentose-Specific Transporters for Activating Dormant Pentose Metabolism in Yarrowia lipolytica.Applied and environmental microbiology · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
L-Xylulose reductases belong to the superfamily of short chain dehydrogenases and reductases (SDRs) and catalyze the NAD(P)H-dependent reduction of L-xylulose to xylitol in L-arabinose and glucuronic acid catabolism. Here we report the identification of a novel L-xylulose reductase LXR3 in the fungus Trichoderma reesei by a bioinformatic approach in combination with a functional analysis. LXR3, a 31 kDa protein, catalyzes the reduction of L-xylulose to xylitol via NADPH and is also able to convert D-xylulose, D-ribulose, L-sorbose, and D-fructose to their corresponding polyols. Transcription of lxr3 is specifically induced by L-arabinose and L-arabitol. Deletion of lxr3 affects growth on L-arabinose and L-arabitol and reduces total NADPH-dependent LXR activity in cell free extracts. A phylogenetic analysis of known L-xylulose reductases shows that LXR3 is phylogenetically different from the Aspergillus niger L-xylulose reductase LxrA and, moreover, that all identified true L-xylulose reductases belong to different clades within the superfamily of SDRs. This indicates that the enzymes responsible for the reduction of L-xylulose in L-arabinose and glucuronic acid catabolic pathways have evolved independently and that even the fungal LXRs of the L-arabinose catabolic pathway have evolved in different clades of the superfamily of SDRs.
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