Article
Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase.
Biochemistry - 12 Apr 2011
Feng Lei, Wanninayake Udayanga, Strom Susan, Geiger James, Walker Kevin D
Abstract excerpt
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...
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