NADPH-dependent 5-keto-D-gluconate reductase is a part of the fungal pathway for D-glucuronate catabolism

Joosu Kuivanen, Peter Richard

    Research output: Contribution to journalArticleScientificpeer-review

    6 Citations (Scopus)

    Abstract

    NADPH-dependent 5-keto-D-gluconate reductase was identified as a missing element in the pathway for D-glucuronate catabolism in fungi. The disruption of the gene, gluF, by CRISPR/Cas9 in the filamentous fungus Aspergillus niger resulted in a strain unable to catabolise D-glucuronate. The purified GluF protein was characterized and kcat and Km values of 23.7 ± 1.8 s-1 and 3.2 ± 0.1 mm for 5-keto-D-gluconate, respectively, were determined. The enzyme is reversible and is active with NADP+ and D-gluconate. We suggest a pathway for D-glucuronate catabolism with the intermediates L-gulonate, 2-keto-L-gulonate, L-idonate, 5-keto-D-gluconate, D-gluconate and D-gluconate-6-phosphate which is a part of the pentose phosphate pathway. A fungal enzyme activity for the conversion of L-gulonate to 2-keto-L-gulonate remains to be identified.

    Original languageEnglish
    Pages (from-to)71-77
    Number of pages7
    JournalFEBS Letters
    Volume592
    Issue number1
    DOIs
    Publication statusPublished - 1 Jan 2018
    MoE publication typeA1 Journal article-refereed

    Keywords

    • 5-keto-gluconate
    • Aspergillus niger
    • CRISPR/Cas9
    • D-gluconate-5-dehydrogenase
    • D-glucuronate
    • EC 1.1.1.69
    • Fungal pathway

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