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February 20, 2026Biochemistry

Rational Design of Plant-Derived Protein Ligases with Altered Substrate Specificity

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Authors

YZYan ZhouSVSimon J. de VeerTTTristan J. Tyler

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Overview

Experiments enhance substrate specificity in engineered asparaginyl ligases, indicating potential for diverse applications.

Key Points

  • The aim is to engineer asparaginyl ligases to expand their substrate specificity for various biochemical applications.
  • Mutated Tyr188 to Ala in OaAEP1 to alter substrate specificity.
  • Produced two additional asparaginyl ligases from different plant families.
  • Examined the effects of corresponding Tyr residue mutations in the S2' pocket.
  • Mutant enzymes showed expanded substrate scope for peptide cyclization and protein-ligation.
  • Established the role of the conserved S2' Tyr residue in determining substrate specificity.
  • Demonstrated successful engineering of ligases with improved transpeptidation capabilities.

Cite This Study

Zhou et al. (2026) studied this question.

synapsesocial.com/papers/6997fa12ad1d9b11b3452f53https://doi.org/10.1021/acs.biochem.5c00808
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