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

3 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

Fingerprint

Glucuronic Acid
NADP
Fungi
Clustered Regularly Interspaced Short Palindromic Repeats
Pentoses
Pentose Phosphate Pathway
Aspergillus niger
Aspergillus
Enzyme activity
Enzymes
Genes
Phosphates
gluconic acid
gluconate 5-dehydrogenase
gulonic acid
Proteins

Keywords

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

Cite this

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title = "NADPH-dependent 5-keto-D-gluconate reductase is a part of the fungal pathway for D-glucuronate catabolism",
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.",
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NADPH-dependent 5-keto-D-gluconate reductase is a part of the fungal pathway for D-glucuronate catabolism. / Kuivanen, Joosu; Richard, Peter.

In: FEBS Letters, Vol. 592, No. 1, 01.01.2018, p. 71-77.

Research output: Contribution to journalArticleScientificpeer-review

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