Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom