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

B. Metz, Dominik Mojzita, S. Herold, C.P. Kubicek, Peter Richard, B. Seiboth (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    12 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
    Number of pages8
    Issue number14
    Publication statusPublished - 2013
    MoE publication typeA1 Journal article-refereed


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