<div class="csl-bib-body">
<div class="csl-entry">Quehenberger, J., Reichenbach, T., Baumann, N., Rettenbacher, L., Divne, C., & Spadiut, O. (2019). Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum. <i>International Journal of Molecular Sciences</i>, <i>20</i>(1), 1–17. https://doi.org/10.3390/ijms20010185</div>
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dc.identifier.issn
1661-6596
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/20058
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dc.description.abstract
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.
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dc.description.sponsorship
Exputec GmbH
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dc.language.iso
en
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dc.publisher
MDPI
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dc.relation.ispartof
International Journal of Molecular Sciences
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dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
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dc.subject
Chaetomium thermophilum
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dc.subject
cofactor binding
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dc.subject
homology model
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dc.subject
kinetics
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dc.subject
stability
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dc.subject
structure
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dc.subject
xylose reductase
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dc.title
Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
