Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from candida tropicalis

Li Chun Chen, Sheng Cih Huang, Phimonphan Chuankhayan, Chung Der Chen, Yen Chieh Huang, Jeyaraman Jeyakanthan, Hsiao Fang Pang, Lee Chung Men, Yu Ching Chen, Yu Kuo Wang, Ming Yih Liu, Tung-Kung Wu*, Chun Jung Chen

*Corresponding author for this work

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Xylose reductase (XR), which requires NADPH as a co-substrate, catalyzes the reduction of d-xylose to xylitol, which is the first step in the metabolism of d - xylose. The detailed three-dimensional structure of XR will provide a better understanding of the biological significance of XR in the efficient production of xylitol from biomass. XR of molecular mass 36.6 kDa from Candida tropicalis was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data from C. tropicalis XR crystals at 2.91 Å resolution, the unit cell belongs to space group P31 or P32. Preliminary analysis indicated the presence of four XR molecules in the asymmetric unit, with 68.0% solvent content.

Original languageEnglish
Pages (from-to)419-421
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number4
DOIs
StatePublished - 15 Apr 2009

Keywords

  • Candida tropicalis
  • Xylose reductase

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    Chen, L. C., Huang, S. C., Chuankhayan, P., Chen, C. D., Huang, Y. C., Jeyakanthan, J., Pang, H. F., Men, L. C., Chen, Y. C., Wang, Y. K., Liu, M. Y., Wu, T-K., & Chen, C. J. (2009). Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from candida tropicalis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(4), 419-421. https://doi.org/10.1107/S1744309109008719