Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.

@article{Yang2009StructuralBA,
  title={Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.},
  author={Liuqing Yang and Marco Hill and Meitian Wang and Santosh Panjikar and Joachim Stoeckigt},
  journal={Angewandte Chemie},
  year={2009},
  volume={48 28},
  pages={
          5211-3
        }
}
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures. 
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