Tryptophan Synthase: Biocatalyst Extraordinaire.

Chembiochem : a European Journal of Chemical Biology
Ella Watkins-DulaneyFrances Arnold

Abstract

Tryptophan synthase (TrpS) has emerged as a paragon of noncanonical amino acid (ncAA) synthesis and is an ideal biocatalyst for synthetic and biological applications. TrpS catalyzes an irreversible, C-C bond-forming reaction between indole and serine to make l-tryptophan; native TrpS complexes possess fairly broad specificity for indole analogues, but are difficult to engineer to extend substrate scope or to confer other useful properties due to allosteric constraints and their heterodimeric structure. Directed evolution freed the catalytically relevant TrpS β-subunit (TrpB) from allosteric regulation by its TrpA partner and has enabled dramatic expansion of the enzyme's substrate scope. This review examines the long and storied career of TrpS from the perspective of its application in ncAA synthesis and biocatalytic cascades.

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Citations

Feb 6, 2021·Biochemical Society Transactions·Wanting Jiao
Feb 25, 2021·Chemical Communications : Chem Comm·Amanda OhlerAdam R Offenbacher
Jun 26, 2021·ACS Catalysis·Reuben B Leveson-GowerGerard Roelfes
Jul 9, 2021·ACS Central Science·Nicholas S SaraiFrances H Arnold
Jul 17, 2021·Angewandte Chemie·Ella J Watkins-DulaneyAndrew R Buller
Aug 13, 2021·Chembiochem : a European Journal of Chemical Biology·Nikolas EspositoNina M Goodey
Sep 8, 2021·Journal of the American Chemical Society·Manfred T Reetz, Marc Garcia-Borràs
Oct 27, 2021·Chembiochem : a European Journal of Chemical Biology·Tyler J DoyonAndrew R Buller

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