April 18, 2024Communications ChemistryOpen Access

Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs

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Engineered asparaginyl ligase OaAEP1-C247A-aa55-351 achieves robust catalytic activity across a broad pH range for site-specific bioconjugation.
Under Fe3+ supplementation, catalytic activity increases 70-fold over parental OaAEP1 and exceeds butelase-1 efficiency by 2-fold.
Structure-based rational design coupled with an optimized nucleophile motif enhances peptide recognition and chemo-enzymatic modification.

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Protein engineering study demonstrates enhanced catalytic activity in engineered asparaginyl ligase OaAEP1, highlighting improved potential for site-specific bioconjugation.

Cite This Study

Tang et al. (2024) studied this question.

synapsesocial.com/papers/68e6e8afb6db643587663b1c https://doi.org/10.1038/s42004-024-01173-8

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Implication

Protein engineering study demonstrates enhanced catalytic activity in engineered asparaginyl ligase OaAEP1, highlighting improved potential for site-specific bioconjugation.

Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs

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Discussion

Implication

Cite This Study

Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs

Key Points

Discussion

Implication

Cite This Study

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