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Tryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active siteTryptophan Synthase beta-subunit from Pyrococcus furiosus with L-threonine non-covalently bound in the active site
Structural highlights
FunctionTRPB1_PYRFU The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). Publication Abstract from PubMedWe report that l-threonine may substitute for l-serine in the beta-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-beta-methyltryptophan (beta-MeTrp) in a single step. The trace activity of the wild-type beta-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this increase is correlated with stabilization of the electrophilic aminoacrylate intermediate. The engineered biocatalyst also reacts with a variety of indole analogues and thiophenol for diastereoselective C-C, C-N, and C-S bond-forming reactions. This new activity circumvents the 3-enzyme pathway that produces beta-MeTrp in nature and offers a simple and expandable route to preparing derivatives of this valuable building block. Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.,Herger M, van Roye P, Romney DK, Brinkmann-Chen S, Buller AR, Arnold FH J Am Chem Soc. 2016 Jul 13;138(27):8388-91. doi: 10.1021/jacs.6b04836. Epub 2016 , Jul 1. PMID:27355405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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