Premium
NADPH‐dependent 5‐keto‐D‐gluconate reductase is a part of the fungal pathway for D‐glucuronate catabolism
Author(s) -
Kuivanen Joosu,
Richard Peter
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12946
Subject(s) - glucuronate , catabolism , pentose phosphate pathway , reductase , gluconic acid , biochemistry , chemistry , enzyme , aspergillus niger , aspergillus nidulans , stereochemistry , metabolic pathway , gene , glycolysis , mutant
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 k cat and K m values of 23.7 ± 1.8 s −1 and 3.2 ± 0.1 m m 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.