Evidence map›Paper›PMID 26377145›Full record

ArticleAngewandte Chemie (International ed. in English)2015

Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis.

Hanna Luhavaya, Marcio V B Dias, Simon R Williams, Hui Hong, Luciana G de Oliveira, Peter F Leadlay

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

6 authors.

Hanna LuhavayaDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA (UK).
Marcio V B DiasDepartment of Microbiology, Institute of Biomedical Science, University of São Paulo, Av. Prof. Lineu Prestes, 1374, 05508-000, São Paulo-SP (Brazil).
Simon R WilliamsUniversity Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK).
Hui HongDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA (UK).
Luciana G de OliveiraDepartment of Organic Chemistry, University of Campinas UNICAMP, Cidade Universitária Zeferino Vaz s/n, P.O. Box 6154, 13083-970, Campinas-SP (Brazil).
Peter F LeadlayDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA (UK). pfl10@cam.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/J007250/1
6 · The paper itself

Abstract

Tetrahydropyran rings are a common feature of complex polyketide natural products, but much remains to be learned about the enzymology of their formation. The enzyme SalBIII from the salinomycin biosynthetic pathway resembles other polyether epoxide hydrolases/cyclases of the MonB family, but SalBIII plays no role in the conventional cascade of ring opening/closing. Mutation in the salBIII gene gave a metabolite in which ring A is not formed. Using this metabolite in vitro as a substrate analogue, SalBIII has been shown to form pyran ring A. We have determined the X-ray crystal structure of SalBIII, and structure-guided mutagenesis of putative active-site residues has identified Asp38 and Asp104 as an essential catalytic dyad. The demonstrated pyran synthase activity of SalBIII further extends the impressive catalytic versatility of α+β barrel fold proteins.

Indexed as

Models, MolecularMolecular ConformationPolyether PolyketidesPolyketide SynthasesPyransStreptomycesPolyether PolyketidesPolyketide SynthasesPyranssalinomycinbiosynthesiscyclasesdehydratasespolyetherspolyketide synthases

Identifiers

PMID26377145
PMCPMC4648038

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.