Characterization of d-xylose reductase, XyrB, from Aspergillus niger

TY - JOUR

T1 - Characterization of d-xylose reductase, XyrB, from Aspergillus niger

AU - Terebieniec, Agata

AU - Chroumpi, Tania

AU - Dilokpimol, Adiphol

AU - Aguilar-Pontes, Maria Victoria

AU - Mäkelä, Miia R

AU - de Vries, Ronald P

N1 - © 2021 The Authors.

PY - 2021/6

Y1 - 2021/6

N2 - d-xylose reductase is a member of the aldo-keto reductase family, and is involved in d-xylose and l-arabinose conversion through the Pentose Catabolic Pathway (PCP) in fungi. In this study, we biochemically characterized a newly identified second d-xylose reductase (XyrB) from Aspergillus niger. This NADPH-dependent reductase is able to efficiently convert d-xylose and l-arabinose, and it has the highest affinity for these sugars of all currently known fungal pentose reductases. A combination of biochemical data, transcriptomics and phylogenetic analysis further illustrated the role of XyrB in the PCP. Enzymes: D-xylose reductase (EC 1.1.1.307), L-arabinose reductase (EC 1.1.1.21).

AB - d-xylose reductase is a member of the aldo-keto reductase family, and is involved in d-xylose and l-arabinose conversion through the Pentose Catabolic Pathway (PCP) in fungi. In this study, we biochemically characterized a newly identified second d-xylose reductase (XyrB) from Aspergillus niger. This NADPH-dependent reductase is able to efficiently convert d-xylose and l-arabinose, and it has the highest affinity for these sugars of all currently known fungal pentose reductases. A combination of biochemical data, transcriptomics and phylogenetic analysis further illustrated the role of XyrB in the PCP. Enzymes: D-xylose reductase (EC 1.1.1.307), L-arabinose reductase (EC 1.1.1.21).

U2 - 10.1016/j.btre.2021.e00610

DO - 10.1016/j.btre.2021.e00610

M3 - Article

C2 - 33842213

SN - 2215-017X

VL - 30

SP - e00610

JO - Biotechnology reports (Amsterdam, Netherlands)

JF - Biotechnology reports (Amsterdam, Netherlands)

ER -