Evidence map›Paper›PMID 28418225›Full record

ArticleAngewandte Chemie (International ed. in English)2017

An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.

Wei Xu, Guifa Zhai, Yuanzhen Liu, Yuan Li, Yanrong Shi, Kui Hong, Hui Hong, Peter F Leadlay, Zixin Deng, Yuhui Sun

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-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

12 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Anti-Foc RT4 Activity of a Newly IsolatedFrontiers in microbiology · 2020
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. 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

10 authors at 2 institutions in 3 countries.

Wei XuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Guifa ZhaiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Yuanzhen LiuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Yuan LiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Yanrong ShiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Kui HongKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Hui HongDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
Peter F LeadlayDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
Zixin DengKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Yuhui SunKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University), Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan, 430071, P.R. China.
Wuhan University · CNBridge University · SS

Funding

Biotechnology and Biological Sciences Research Council BB/I002413/1
6 · The paper itself

Abstract

Detailed analysis of the modular Type I polyketide synthase (PKS) involved in the biosynthesis of the marginolactone azalomycin F in mangrove Streptomyces sp. 211726 has shown that only nineteen extension modules are required to accomplish twenty cycles of polyketide chain elongation. Analysis of the products of a PKS mutant specifically inactivated in the dehydratase domain of extension-module 1 showed that this module catalyzes two successive elongations with different outcomes. Strikingly, the enoylreductase domain of this module can apparently be "toggled" off and on : it functions in only the second of these two cycles. This novel mechanism expands our understanding of PKS assembly-line catalysis and may explain examples of apparent non-colinearity in other modular PKS systems.

Indexed as

MacrolidesMolecular ConformationMutationOxidoreductasesPolyketide Synthasesazalomycin-FMacrolidesOxidoreductasesPolyketide Synthasesantibioticsbiosynthesisenoylreductasesiteration modulesmacrocyclic polyketides

Identifiers

PMID28418225
PMCPMC5518293
OpenAlexW2605597117

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.