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Related Experiment Video

Updated: Mar 19, 2026

Author Spotlight: Characterizing Novel Enzymes from Extremophiles and Common Pathogens to Understand DNA Repair and Replication

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Published on: July 5, 2024

Recent advances in sortase-catalyzed ligation methodology.

John M Antos¹, Matthias C Truttmann², Hidde L Ploegh²

¹Department of Chemistry, Western Washington University, 516 High Street, Bellingham, WA 98229, USA.

Current Opinion in Structural Biology

|June 20, 2016

Summary

Bacterial sortase enzymes are increasingly used for creating new protein derivatives. Recent advancements improve sortase reaction efficiency, scope, and compatibility for diverse applications, including structural biology.

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Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Bacterial sortases catalyze transpeptidation reactions, enabling protein ligation.
The application of sortase-mediated protein conjugation is expanding.
Methodological advancements are enhancing sortase reaction efficiency and substrate scope.

Purpose of the Study:

To provide an overview of recent developments in sortase-based strategies.
To highlight improvements in sortase reaction performance and scope.
To discuss applications of sortase technology in structural biology.

Main Methods:

Review of engineered sortases for increased catalytic rates.
Analysis of redesigned acyl donors and acceptors to reduce reaction reversibility.
Examination of strategies for broadening substrate compatibility.

Main Results:

Engineered sortases demonstrate enhanced reaction kinetics.
Modified substrates improve the efficiency and directionality of sortase reactions.
New strategies expand the utility of sortase ligation for diverse protein targets.

Conclusions:

Sortase-mediated protein engineering is a rapidly evolving field with significant potential.
Ongoing methodological improvements are broadening the applicability of sortase technology.
These advancements facilitate novel applications in protein modification and structural biology.