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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
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Related Experiment Video

Updated: Jan 17, 2026

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
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PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

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Sequence-based generative AI design of versatile tryptophan synthases.

Théophile Lambert1,2, Amin Tavakoli3, Gautham Dharuman4

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.

Nature Communications
|January 14, 2026
PubMed
Summary
This summary is machine-generated.

Generative protein language models can create novel enzymes, like tryptophan synthase beta-subunits (TrpB), that are stable, active, and even outperform natural enzymes. This breakthrough accelerates biocatalyst discovery and engineering for sustainable applications.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Computational Biology

Background:

  • Enzyme discovery and optimization are crucial for sustainable chemistry but face bottlenecks in identifying suitable starting points.
  • Designing diverse and functional enzyme libraries remains a significant challenge in biocatalysis.

Purpose of the Study:

  • To utilize a protein language model (GenSLM) for generating novel beta-subunit of tryptophan synthase (TrpB) enzymes.
  • To assess the stability, catalytic activity, and substrate promiscuity of these generated TrpB enzymes.
  • To demonstrate the potential of generative models in biocatalyst discovery and engineering.

Main Methods:

  • Application of the GenSLM protein language model to design novel TrpB enzyme sequences.
  • Expression and characterization of generated TrpB enzymes in Escherichia coli.
  • Evaluation of enzyme stability, catalytic activity, and substrate promiscuity on native and non-native substrates.

Main Results:

  • Successfully generated novel TrpB enzymes that express functional proteins in E. coli.
  • Many generated TrpBs exhibited high stability and catalytic activity.
  • Significant substrate promiscuity was observed, with some variants outperforming natural TrpBs and even laboratory-evolved enzymes.
  • Comparison with natural homologs confirmed the acquisition of non-natural properties by generated enzymes.

Conclusions:

  • Generative protein language models can create enzymes that retain natural functions while acquiring novel properties.
  • These models represent powerful tools for accelerating biocatalyst discovery and engineering.
  • The generated TrpBs demonstrate enhanced versatility, opening new avenues for enzymatic applications.