Evidence map›Paper›PMID 27463729›Full record

ReviewAntibiotics (Basel, Switzerland)2016

Biotin Protein Ligase Is a Target for New Antibacterials.

Jiage Feng, Ashleigh S Paparella, Grant W Booker, Steven W Polyak, Andrew D Abell

Open access · goldAbstract readReview
In one paragraph

Review in Antibiotics (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025
    Review
  5. New Potent Sulfonamide-Based Inhibitors ofACS medicinal chemistry letters · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
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

5 authors at 1 institution in 1 country.

Jiage FengDepartment of Chemistry, University of Adelaide, North Tce, Adelaide, SA 5005, Australia. dovekey_feng@hotmail.com.
Ashleigh S PaparellaSchool of Biological Sciences, University of Adelaide, North Tce, Adelaide, SA 5005, Australia. ashleigh.paparella@adelaide.edu.au.
Grant W BookerSchool of Biological Sciences, University of Adelaide, North Tce, Adelaide, SA 5005, Australia. grant.booker@adelaide.edu.au.
Steven W PolyakSchool of Biological Sciences, University of Adelaide, North Tce, Adelaide, SA 5005, Australia. steven.polyak@adelaide.edu.au.
Andrew D AbellSchool of Biological Sciences, University of Adelaide, North Tce, Adelaide, SA 5005, Australia. andrew.abell@adelaide.edu.au.
The University of Adelaide · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is a desperate need for novel antibiotic classes to combat the rise of drug resistant pathogenic bacteria, such as Staphylococcus aureus. Inhibitors of the essential metabolic enzyme biotin protein ligase (BPL) represent a promising drug target for new antibacterials. Structural and biochemical studies on the BPL from S. aureus have paved the way for the design and development of new antibacterial chemotherapeutics. BPL employs an ordered ligand binding mechanism for the synthesis of the reaction intermediate biotinyl-5'-AMP from substrates biotin and ATP. Here we review the structure and catalytic mechanism of the target enzyme, along with an overview of chemical analogues of biotin and biotinyl-5'-AMP as BPL inhibitors reported to date. Of particular promise are studies to replace the labile phosphoroanhydride linker present in biotinyl-5'-AMP with alternative bioisosteres. A novel in situ click approach using a mutant of S. aureus BPL as a template for the synthesis of triazole-based inhibitors is also presented. These approaches can be widely applied to BPLs from other bacteria, as well as other closely related metabolic enzymes and antibacterial drug targets.

Indexed as

antibioticbiotinbiotin protein ligaseinhibitor designin situ click chemistryStaphylococcus aureusX-ray crystallography

Identifiers

PMID27463729
PMCPMC5039522
OpenAlexW2476162872

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.