Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis.

@article{Felicetti2004AristolocheneSM,
  title={Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis.},
  author={Brunella Felicetti and David E Cane},
  journal={Journal of the American Chemical Society},
  year={2004},
  volume={126 23},
  pages={7212-21}
}
Incubation of farnesyl diphosphate (1) with Penicillium roqueforti aristolochene synthase yielded (+)-aristolochene (4), accompanied by minor quantities of the proposed intermediate (S)-(-)germacrene A (2) and the side-product (-)-valencene (5) in a 94:4:2 ratio. By contrast, the closely related aristolochene synthase from Aspergillus terreus cyclized farnesyl diphosphate only to (+)-aristolochene (4). Site-directed mutagenesis of amino acid residues in two highly conserved Mg(2+)-binding… CONTINUE READING

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