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Updated: Feb 27, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Identification of sortase substrates by specificity profiling.

Lena Schmohl¹, Jan Bierlmeier¹, Nicolai von Kügelgen¹

¹Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Str. 4, D-72076 Tuebingen, Germany.

Bioorganic & Medicinal Chemistry

|July 8, 2017

Summary

This summary is machine-generated.

Sortases attach surface proteins in gram-positive bacteria. Streptococci sortases show relaxed specificity, preferring LPKLG over LPKTG motifs, enhancing their use in protein chemistry.

Keywords:

Protein labeling Sortase Sortase-mediated ligation Staphylococcus aureus Streptococcus pyogenes

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Last Updated: Feb 27, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

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Published on: May 25, 2018

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

Biochemistry
Microbiology
Protein Chemistry

Background:

Sortases are enzymes crucial for anchoring surface proteins to the peptidoglycan layer in gram-positive bacteria.
They function by cleaving a donor substrate at the LPxTG motif and ligating it to an acceptor protein.
Sortase A from Staphylococcus aureus is well-characterized, with homologs found across various gram-positive bacteria.

Purpose of the Study:

To investigate and compare the substrate specificity of sortases from Staphylococci and Streptococci species.
To determine if differences in specificity could be exploited for novel applications in protein chemistry.

Main Methods:

Profiling the substrate specificity of seven different sortase enzymes.
Analyzing donor and acceptor substrate preferences for Staphylococci and Streptococci sortases.
Comparing the canonical LPxTG motif recognition with observed preferences.

Main Results:

Sortases from Streptococci exhibited broader, more relaxed specificity for both donor and acceptor substrates compared to Staphylococci sortases.
Specifically, Streptococci sortases demonstrated a preference for an LPKLG donor substrate sequence over the canonical LPKTG motif.
This relaxed specificity suggests potential for greater versatility in enzymatic applications.

Conclusions:

The distinct substrate specificities of Streptococci sortases, particularly their preference for LPKLG, offer new opportunities for protein engineering.
These findings expand the utility of sortases as powerful tools in protein chemistry, enabling more flexible substrate ligation.
Further research can leverage these properties for advanced applications in biotechnology and synthetic biology.