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Open AccessArticle

Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum

1
Research Division Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Faculty of Technical Chemistry, TU Wien, 1060 Vienna, Austria
2
KTH School of Engineering Sciences in Chemistry, Biotechnology and Health, SE-100 44 Stockholm, Sweden
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(1), 185; https://doi.org/10.3390/ijms20010185
Received: 10 December 2018 / Revised: 29 December 2018 / Accepted: 1 January 2019 / Published: 6 January 2019
(This article belongs to the Special Issue Industrial Enzymes: Structure, Function and Applications)
While in search of an enzyme for the conversion of xylose to xylitol at elevated temperatures, a xylose reductase (XR) gene was identified in the genome of the thermophilic fungus Chaetomium thermophilum. The gene was heterologously expressed in Escherichia coli as a His6-tagged fusion protein and characterized for function and structure. The enzyme exhibits dual cofactor specificity for NADPH and NADH and prefers D-xylose over other pentoses and investigated hexoses. A homology model based on a XR from Candida tenuis was generated and the architecture of the cofactor binding site was investigated in detail. Despite the outstanding thermophilicity of its host the enzyme is, however, not thermostable. View Full-Text
Keywords: xylose reductase; Chaetomium thermophilum; kinetics; structure; homology model; cofactor binding; stability xylose reductase; Chaetomium thermophilum; kinetics; structure; homology model; cofactor binding; stability
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Quehenberger, J.; Reichenbach, T.; Baumann, N.; Rettenbacher, L.; Divne, C.; Spadiut, O. Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum. Int. J. Mol. Sci. 2019, 20, 185.

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