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Microbial transglutaminase displays broad acyl-acceptor substrate specificity.

Maria T Gundersen1, Jeffrey W Keillor, Joelle N Pelletier

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Microbial transglutaminase (MTG) efficiently forms amide bonds. This study reveals MTG accepts diverse, short, and clickable substrates, expanding biocatalytic applications for peptide and protein modification.

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Protein Chemistry and Modification
  • Industrial Biotechnology

Background:

  • Amide bond formation is crucial in industrial synthesis.
  • Microbial transglutaminase (MTG) is a key enzyme for protein crosslinking in food and textiles.
  • MTG typically catalyzes reactions between glutamine and lysine side chains.

Purpose of the Study:

  • To explore short and chemically diverse acyl-acceptor substrates for MTG.
  • To understand the tolerance of MTG to nonnatural substrates.
  • To expand the biocatalytic applications of MTG through substrate diversification.

Main Methods:

  • Investigated the reactivity of various short-chain alkyl-based amino acids and esterified α-amino acids as MTG acyl-acceptor substrates.
  • Tested nonnatural compounds, including those with cyclic and aromatic amine groups.
  • Evaluated small amines containing azide or alkyne groups for click chemistry compatibility.

Main Results:

  • Demonstrated that glycine and several esterified α-amino acids (Thr, Ser, Cys, Trp) act as MTG acceptor substrates.
  • Identified that amines with less steric hindrance and aromatic rings near the amine group enhance reactivity.
  • Showcased high reactivity of azide- and alkyne-containing amines, enabling 'clickable' peptide synthesis.

Conclusions:

  • MTG exhibits broad tolerance for chemically diverse natural and nonnatural acyl-acceptor substrates.
  • This expands the utility of MTG for modifying glutamine-containing peptides and proteins.
  • The findings provide a robust method for creating minimally modified, 'clickable' peptides.