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  • 标题:Structural insight into D-xylose utilization by xylose reductase from Scheffersomyces stipitis
  • 本地全文:下载
  • 作者:Hyeoncheol Francis Son ; Sun-Mi Lee ; Kyung-Jin Kim
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2018
  • 卷号:8
  • 期号:1
  • 页码:17442
  • DOI:10.1038/s41598-018-35703-x
  • 语种:English
  • 出版社:Springer Nature
  • 摘要:-xylose reductase from Schefferzomyces stipitis (SsXR) at a 1.95 Å resolution. We also determined the SsXR structure in complex with the NADPH cofactor and revealed that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. Phylogenetic tree analysis showed that AKR enzymes annotated with bacterial/archaeal XRs belonged to uncharacterized AKR families and might have no XR function, and yeast/fungi derived enzymes, which belong to the same group with SsXR, can be candidates for XR to increase xylose consumption.
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