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

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 c...

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Autores principales: Quehenberger, Julian, Reichenbach, Tom, Baumann, Niklas, Rettenbacher, Lukas, Divne, Christina, Spadiut, Oliver
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337131/
https://www.ncbi.nlm.nih.gov/pubmed/30621365
http://dx.doi.org/10.3390/ijms20010185
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author Quehenberger, Julian
Reichenbach, Tom
Baumann, Niklas
Rettenbacher, Lukas
Divne, Christina
Spadiut, Oliver
author_facet Quehenberger, Julian
Reichenbach, Tom
Baumann, Niklas
Rettenbacher, Lukas
Divne, Christina
Spadiut, Oliver
author_sort Quehenberger, Julian
collection PubMed
description 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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spelling pubmed-63371312019-01-22 Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum Quehenberger, Julian Reichenbach, Tom Baumann, Niklas Rettenbacher, Lukas Divne, Christina Spadiut, Oliver Int J Mol Sci Article 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. MDPI 2019-01-06 /pmc/articles/PMC6337131/ /pubmed/30621365 http://dx.doi.org/10.3390/ijms20010185 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Quehenberger, Julian
Reichenbach, Tom
Baumann, Niklas
Rettenbacher, Lukas
Divne, Christina
Spadiut, Oliver
Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title_full Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title_fullStr Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title_full_unstemmed Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title_short Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum
title_sort kinetics and predicted structure of a novel xylose reductase from chaetomium thermophilum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337131/
https://www.ncbi.nlm.nih.gov/pubmed/30621365
http://dx.doi.org/10.3390/ijms20010185
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