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taxus canadensis/fenilalanina
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Insight into the mechanism of aminomutase reaction: a case study of phenylalanine aminomutase by computational approach.
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The Taxus canadensis phenylalanine aminomutase (TcPAM) catalyze the isomerization of (S)-α-phenylalanine to the (R)-β-isomer. The active site of TcPAM contains the signature 5-methylene-3,5-dihydroimidazol-4-one (MIO) prosthesis, observed in the ammonia lyase class of enzymes. Up to now, there are
Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase.
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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)-Styryl-α-alanine used to probe the intermolecular mechanism of an intramolecular MIO-aminomutase.
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A Taxus canadensis phenylalanine aminomutase (TcPAM) catalyzes the isomerization of (S)-α- to (R)-β-phenylalanine, making (E)-cinnamate (~10%) as a byproduct at steady state. A currently accepted mechanism for TcPAM suggests that the amino group is transferred from the substrate to a prosthetic
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