Evidence map›Paper›PMID 33290621›Full record

ReviewChembiochem : a European journal of chemical biology2021

Engineered Sortases in Peptide and Protein Chemistry.

Christian Freund, Dirk Schwarzer

Open access · hybridAbstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Sortase-Mediated Multi-Fragment Assemblies by Ligation Site Switching.Angewandte Chemie (International ed. in English) · 2022
    Article
  17. Article
  18. Review
  19. Review
  20. Engineered Sortases in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Christian FreundFreie Universität Berlin, Institute of Chemistry and Biochemistry, Thielallee 63, 14195, Berlin, Germany.ORCID 0000-0001-7416-8226
Dirk SchwarzerUniversity of Tübingen, Interfaculty Institute of Biochemistry (IFIB), Auf der Morgenstelle 34, 72076, Tübingen, Germany.
Freie Universität Berlin · DEUniversity of Tübingen · DE

Funding

priority program SPP 1623 of the Deutsche Forschungsgemeinschaft FR-1325/15-1 (CF)priority program SPP 1623 of the Deutsche Forschungsgemeinschaft SCHW 1163/7-1 (DS)
6 · The paper itself

Abstract

The transpeptidase sortase A of Staphylococcus aureus (Sa-SrtA) is a valuable tool in protein chemistry. The native enzyme anchors surface proteins containing a highly conserved LPxTG sorting motif to a terminal glycine residue of the peptidoglycan layer in Gram-positive bacteria. This reaction is exploited for sortase-mediated ligation (SML), allowing the site-specific linkage of synthetic peptides and recombinant proteins by a native peptide bond. However, the moderate catalytic efficiency and specificity of Sa-SrtA fueled the development of new biocatalysts for SML, including the screening of sortase A variants form microorganisms other than S. aureus and the directed protein evolution of the Sa-SrtA enzyme itself. Novel display platforms and screening formats were developed to isolate sortases with altered properties from mutant libraries. This yielded sortases with strongly enhanced catalytic activity and enzymes recognizing new sorting motifs as substrates. This minireview focuses on recent advances in the field of directed sortase evolution and applications of these tailor-made enzymes in biochemistry.

Indexed as

Protein EngineeringAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesPeptidesRecombinant ProteinsStaphylococcus aureusAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesPeptidesRecombinant Proteinssortase Aprotein bioconjugationprotein engineeringprotein semisynthesissortasestranspeptidases

Identifiers

PMID33290621
PMCPMC8248031
OpenAlexW3111855658

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.