Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa.
A xylose reductase (XR) gene was identified from the Neurospora crassa whole-genome sequence, expressed heterologously in Escherichia coli, and purified as a His6-tagged fusion in high yield. This enzyme is one of the most active XRs thus far characterized and may be used for the in vitro production of xylitol.
Woodyer
Ryan
R
Department of Chemistry, University of Illinois at Urbana-Champaign, 600 S. Mathews Ave., Urbana, IL 61801, USA.
Simurdiak
Michael
M
van der Donk
Wilfred A
WA
Zhao
Huimin
H
D000449:Aldehyde Reductase / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005800:Genes, Fungal; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D008970:Molecular Weight; D009492:Neurospora crassa / Q000201:enzymology* / Q000235:genetics*; D020836:Protein Structure, Quaternary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature; D014993:Xylitol / Q000096:biosynthesis
D011993:Recombinant Fusion Proteins; D000449:Aldehyde Reductase; D014993:Xylitol