| Literature DB >> 19342796 |
Li Chun Chen1, 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.
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 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicated the presence of four XR molecules in the asymmetric unit, with 68.0% solvent content.Entities:
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Year: 2009 PMID: 19342796 PMCID: PMC2664776 DOI: 10.1107/S1744309109008719
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091