The β-subunit of tryptophan synthase is a latent tyrosine synthase

We thank the following past and present members of the Arnold Laboratory for helpful discussions on the manuscript and experimental assistance: A. Buller, T. Boville, D. Romney, E. Watkins-Dulaney, S. Brinkmann-Chen and N. Goldberg, among many others. We thank S. Du for helpful discussions and J. Kaiser from the Caltech Molecular Observatory for crystallography support. This work was supported by the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under award R01GM125887. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. Individual support comes from Nagendranath Reddy Graduate Fellowship (to P.J.A.); Caltech Biotechnology Leadership Program (BLP; NIH training grant 5T32GM112592-5 to K.E.J.); Caltech AI4Science/Amazon AWS Fellowship (to K.E.J.); Merck–Helen Hay Whitney Postdoctoral Fellowship (to N.J.P.); Ruth L. Kirschstein NIH Postdoctoral Fellowship (1F32GM143797-01A1 to J.L.K.); National Science Foundation Graduate Research Fellowship Program (GRFP; grant DGE‐1745301 to V.C.B.); Fonds de recherche du Québec Nature et technologie (FRQNT; to J.D.). The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript.

All data, including the 18,719 annotated TrpB-like sequences, are available in the main text or supplementary materials. Full protein crystallographic data have been deposited with the PDB (https://www.rcsb.org) under accession codes 8EGY, 8EGZ, 8EH0 and 8EH1. Source data are provided with this paper.

P.J.A. and F.H.A. are inventors on patent applications filed by the California Institute of Technology that cover enzymatic synthesis of tyrosine analogs from analogs of phenol and serine (US17/985,033 and PCT/US2022/049617, pending). The other authors declare no competing interests.