A novel L-xylulose reductase essential for L-arabinose catabolism in Trichoderma reesei

Benjamin Metz, Dominik Mojzita, Silvia Herold, Christian P. Kubicek, Peter Richard, Bernard Seiboth (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    16 Citations (Scopus)


    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.
    Original languageEnglish
    Pages (from-to)2453-2460
    Issue number14
    Publication statusPublished - 2013
    MoE publication typeA1 Journal article-refereed


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