4.8 Article

Characterization of QmnD3/QmnD4 for Double Bond Formation in Quartromicin Biosynthesis

Journal

ORGANIC LETTERS
Volume 16, Issue 6, Pages 1578-1581

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ol500111n

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Funding

  1. 973 Program [2010CB833200, 2012CB721100]
  2. NSFC [21072214, 31330003]

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In this work, two enzymes responsible for the biogenesis of possible [4 + 2] reaction precursors in the quartromicin biosynthetic pathway were characterized: acetylation of 1 to yield 2 was catalyzed by QmnD3, and subsequent acetic acid elimination of 2 to form double bond product 3 was catalyzed by QmnD4. Site-directed mutagenesis assay of QmnD3 and QmnD4 was investigated, and a general base-catalyzed mechanism for QmnD4 is proposed.

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