California Institute of Technology

Andrew Richard Buller

David K Romney

Sabine Brinkmann-Chen

Christina E Boville

Christopher K Prier

Philipp Koch

Remkes A Scheele

Javier Murciano Calles

Michael Herger

Paul Van Roye

The present disclosure provides methods for preparing β-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a β-substituted serine, and iii) a tryptophan synthase β-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the β-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new β-substituted tryptophan analogs are also described.

Methods and enzyme catalysts for the synthesis of non-canonical amino acids

This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.

Engineered beta-subunit of tryptophan synthase for production of non-canonical amino acids

The present disclosure provides methods for preparing &#x3b2;-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a &#x3b2;-substituted serine, and iii) a tryptophan synthase &#x3b2;-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the &#x3b2;-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new &#x3b2;-substituted tryptophan analogs are also described.

Beta-substituted non-canonical amino acids

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Pasadena, CA, United States of America

Andrew Richard Buller