Structural highlights
Function
[TRPB1_PYRFU] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity).
Publication Abstract from PubMed
We 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.
References
- ↑ Herger M, van Roye P, Romney DK, Brinkmann-Chen S, Buller AR, Arnold FH. Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase. J Am Chem Soc. 2016 Jul 13;138(27):8388-91. doi: 10.1021/jacs.6b04836. Epub 2016 , Jul 1. PMID:27355405 doi:http://dx.doi.org/10.1021/jacs.6b04836
