title: Heterologous expression, purification, and characterization of xylose reductase from Candida shehatae.
abstract: 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.
authors.affiliation: Institute of Industrial Biotechnology, Huaqiao University, 362021, Quanzhou, P.R. China.
authors.forename: Xiaoxia
authors.initials: X
authors.lastname: Wang
authors.forename: Baishan
authors.initials: B
authors.lastname: Fang
authors.forename: Juxiang
authors.initials: J
authors.lastname: Luo
authors.forename: Wenjun
authors.initials: W
authors.lastname: Li
authors.forename: Liaoyuan
authors.initials: L
authors.lastname: Zhang
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; D000449:Aldehyde Reductase