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Enhancing Enzymatic Bioconjugation Efficiency via Computer-Based Installation of a Substrate Recruitment Domain.

Christopher Shelby¹, Kaylee P Kuzelka², Jonathan M Ellis³

¹Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, United States.

Bioconjugate Chemistry

|March 17, 2026

Summary

This summary is machine-generated.

Computational design created a new enzyme, design42 (D42), that precisely links molecules to proteins. This enzyme targets specific recognition sequences, enabling controlled bioconjugation for applications like antibody-drug development.

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Area of Science:

Bioconjugation chemistry
Protein engineering
Enzyme catalysis

Background:

Enzyme-mediated bioconjugation offers mild and efficient methods for creating protein conjugates.
Promiscuous enzymes can modify diverse substrates but risk off-target reactions.
Controlling enzyme specificity is crucial for precise bioconjugation.

Purpose of the Study:

To engineer a promiscuous enzyme, tyrosinase, for targeted substrate modification.
To develop a computational design strategy for enhancing enzyme specificity.
To create a novel bioconjugation system for precise protein modification.

Main Methods:

Computational design was used to install a substrate recruitment domain (SRD) onto tyrosinase.
The redesigned enzyme, design42 (D42), was engineered to recognize a specific 6-amino acid recognition sequence (RS).
D42 mediates the conversion of tyrosine residues adjacent to the RS into orthoquinones for subsequent nucleophilic modification.

Main Results:

The engineered D42 enzyme demonstrated preferential modification of tyrosine residues within the context of the SRD-bound recognition sequence.
This targeted modification allows for selective functionalization of peptides and proteins.
The system was successfully applied to install cytotoxic molecules onto a monoclonal antibody.

Conclusions:

The D42 enzyme provides a highly specific and efficient bioconjugation platform.
This computational design approach enables precise control over enzyme activity and substrate targeting.
The developed system has significant potential for therapeutic applications, including antibody-drug conjugate development.