Heterologous expression, purification, and characterization of xylose reductase from Candida shehatae.
The xylose reductase (XR) gene (xyl1) from Candida shehatae was cloned and expressed in Escherichia coli, and purified as a His(6)-tagged fusion protein. The recombinant XR had K(m) values for NADH than NADPH of 150 microM and 20 microM, respectively. The optimal reaction was at pH 6.5 and 35 degrees C. The enzyme was specific for D-xylese.
Wang
Xiaoxia
X
Institute of Industrial Biotechnology, Huaqiao University, 362021, Quanzhou, P.R. China.
Fang
Baishan
B
Luo
Juxiang
J
Li
Wenjun
W
Zhang
Liaoyuan
L
D000449:Aldehyde Reductase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002175:Candida / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular / Q000379:methods; D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D011994:Recombinant Proteins; D000449:Aldehyde Reductase