Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase
…, U Wanninayake, S Strom, J Geiger, KD Walker
Index: Feng, Lei; Wanninayake, Udayanga; Strom, Susan; Geiger, James; Walker, Kevin D. Biochemistry, 2011 , vol. 50, # 14 p. 2919 - 2930
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Citation Number: 29
Abstract
The structure of a phenylalanine aminomutase (Tc PAM) from Taxus canadensis has been determined at 2.4 Å resolution. The active site of the Tc PAM contains the signature 4- methylidene-1 H-imidazol-5 (4 H)-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 Tc PAM reaction product is ...
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