Analysis of UDP-D-apiose/UDP-D-xylose synthase-catalyzed conversion of UDP-D-apiose phosphonate to UDP-D-xylose phosphonate: Implications for a retroaldol-aldol mechanism

Sei Hyun Choi, Steven O. Mansoorabadi, Yung Nan Liu, Tun Cheng Chien, Hung Wen Liu

研究成果: 雜誌貢獻文章

17 引文 斯高帕斯(Scopus)

摘要

UDP-d-apiose/UDP-d-xylose synthase (AXS) catalyzes the conversion of UDP-d-glucuronic acid to UDP-d-apiose and UDP-d-xylose. An acetyl-protected phosphonate analogue of UDP-d-apiose was synthesized and used in an in situ HPLC assay to demonstrate for the first time the ability of AXS to interconvert the two reaction products. Density functional theory calculations provided insight into the energetics of this process and the apparent inability of AXS to catalyze the conversion of UDP-d-xylose to UDP-d-apiose. The data suggest that this observation is unlikely to be due to an unfavorable equilibrium but rather results from substrate inhibition by the most stable chair conformation of UDP-d-xylose. The detection of xylose cyclic phosphonate as the turnover product reveals significant new details about the AXS-catalyzed reaction and supports the proposed retroaldol-aldol mechanism of catalysis.

原文英語
頁(從 - 到)13946-13949
頁數4
期刊Journal of the American Chemical Society
134
發行號34
DOIs
出版狀態已發佈 - 2012 八月 29

    指紋

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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