Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase.

@article{Feng2011MechanisticMA,
  title={Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase.},
  author={Lei Feng and Udayanga S Wanninayake and Susan Strom and James Geiger and Kevin C. Walker},
  journal={Biochemistry},
  year={2011},
  volume={50 14},
  pages={2919-30}
}
The structure of a phenylalanine aminomutase (TcPAM) from Taxus canadensis has been determined at 2.4 Å resolution. The active site of the TcPAM contains the signature 4-methylidene-1H-imidazol-5(4H)-one prosthesis, observed in all catalysts of the class I lyase-like family. This catalyst isomerizes (S)-α-phenylalanine to the (R)-β-isomer by exchange of the NH2/H pair. The stereochemistry of the TcPAM reaction product is opposite of the (S)-β-tyrosine made by the mechanistically related… CONTINUE READING