title: [Homology modeling and molecular docking of xylitol dehydrogenase from Aspergillus Oryzae].
abstract: OBJECTIVE
  We investigated the structure model and function of xylitol dehydrogenase from Aspergillus oryzae.
  
  
  METHODS
  Xylitol dehydrogenase (XDH) gene from Aspergillus oryzae was cloned and sequenced. We constructed four tertiary structure models of XDH by homology modeling with Swiss-MODEL and Modeller and obtained the best quality model by evaluation of PROCHECK and Prosa2003. The dockings of NAD+, Zn2+ and xylitol with XDH were performed by Molsoft program.
  
  
  RESULTS
  Structure analysis suggested that XDH was a member of medium-chain dehydrogenase/reductase (MDR) family. This was supported by the presence of the zinc-containing alcohol dehydrogenase signature and a typical alcohol dehydrogenase Rossmann fold pattern composed by NAD+ binding domain present in MDR superfamily. The molecular docking indicated that amino acid residues Asp206, Arg211, Ser255, Ser301 and Arg303 in XDH binding domain had hydrogen bonding with NAD+, His72 and Glu73 in catalytic domain had hydrogen bonding with Zn2+, Ile46, Ile349, Lys350 and Thr351 in catalytic domain had hydrogen bonding with xylitol.
  
  
  CONCLUSIONS
  These key amino acid residues might play a vital role in the XDH catalytic reaction and can instruct the further directed modification of XDH.
authors: Department of Bioengineering & Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen 361021, China. chenhw@hqu.edu.cn
authors: Hongwen
authors: H
authors: Chen
authors: Yuanbo
authors: Y
authors: Gou
authors: Ka
authors: K
authors: Zhang
authors: Baishan
authors: B
authors: Fang
mesh_terms: D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000201:enzymology*; D020134:Catalytic Domain; D050542:D-Xylulose Reductase / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data
chemical_list: D050542:D-Xylulose Reductase