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Showing 1–3 of 3 results
Advanced filters: Author: Vignesh Bhethanabotla Clear advanced filters
  • Enzymes are highly selective and sustainable catalysts for chemical synthesis, but their optimization is often limited by the difficulty of identifying functional starting points. This study shows that using the GenSLM protein language model to design TrpB variants can yield stable, active enzymes with broad substrate promiscuity, outperforming natural and evolved counterparts and demonstrating the potential of generative models to accelerate biocatalyst discovery.

    • Théophile Lambert
    • Amin Tavakoli
    • Frances H. Arnold
    ResearchOpen Access
    Nature Communications
    P: 1-12
  • Biochemical pathways for aromatic amino acid synthesis are ancient and highly conserved. Directed evolution of the β-subunit of tryptophan synthase (TrpB)—a proficient biocatalyst that converts indole to l-tryptophan—enabled this enzyme to make l-tyrosines from phenols, a pathway not (yet) known in nature.

    • Patrick J. Almhjell
    • Kadina E. Johnston
    • Frances H. Arnold
    Research
    Nature Chemical Biology
    Volume: 20, P: 1086-1093