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The pentose catabolic pathway of the rice‐blast fungus Magnaporthe oryzae involves a novel pentose reductase restricted to few fungal species
Author(s) -
Klaubauf Sylvia,
Ribot Cecile,
Melayah Delphine,
Lagorce Arnaud,
Lebrun Marc-Henri,
de Vries Ronald P.
Publication year - 2013
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 - 10.1016/j.febslet.2013.03.003
Subject(s) - pentose , pentose phosphate pathway , fungus , biochemistry , magnaporthe grisea , catabolism , biology , magnaporthe , chemistry , enzyme , microbiology and biotechnology , botany , oryza sativa , fermentation , glycolysis , gene
A gene ( MoPRD1 ), related to xylose reductases, was identified in Magnaporthe oryzae . Recombinant MoPRD1 displays its highest specific reductase activity toward l ‐arabinose and d ‐xylose. K m and V max values using l ‐arabinose and d ‐xylose are similar. MoPRD1 was highly overexpressed 2–8 h after transfer of mycelium to d ‐xylose or l ‐arabinose, compared to d ‐glucose. Therefore, we conclude that MoPDR1 is a novel pentose reductase, which combines the activities and expression patterns of fungal l ‐arabinose and d ‐xylose reductases. Phylogenetic analysis shows that PRD1 defines a novel family of pentose reductases related to fungal d ‐xylose reductases, but distinct from fungal l ‐arabinose reductases. The presence of PRD1, l ‐arabinose and d ‐xylose reductases encoding genes in a given species is variable and likely related to their life style.