Biochemical characterization of an L-Xylulose reductase from Neurospora crassa.
An l-xylulose reductase identified from the genome sequence of the filamentous fungus Neurospora crassa was heterologously expressed in Escherichia coli as a His(6) tag fusion protein, purified, and characterized. The enzyme may be used in the production of xylitol from the major pentose components of hemicellulosic waste, d-xylose and l-arabinose.
Nair
Nikhil
N
Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, 215 RAL, Box C3, 600 S. Mathews Ave., Urbana, IL 61801, USA.
Zhao
Huimin
H
D003001:Cloning, Molecular; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D009492:Neurospora crassa / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D013696:Temperature; D014993:Xylitol / Q000378:metabolism
D011994:Recombinant Proteins; D013401:Sugar Alcohol Dehydrogenases; C023300:L-xylulose reductase; D014993:Xylitol