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RSS FeedsIJMS, Vol. 20, Pages 185: Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum (International Journal of Molecular Sciences)

 
 

7 january 2019 09:00:05

 
IJMS, Vol. 20, Pages 185: Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum (International Journal of Molecular Sciences)
 




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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27 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
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