Evidence map›Paper›PMID 27346052›Full record

ArticleChemical communications (Cambridge, England)2016

α-Methylation follows condensation in the gephyronic acid modular polyketide synthase.

Drew T Wagner, D Cole Stevens, M Rachel Mehaffey, Hannah R Manion, Richard E Taylor, Jennifer S Brodbelt, Adrian T Keatinge-Clay

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PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical communications (Cambridge, England), 2016. 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
4.6field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Drew T WagnerDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA. adriankc@utexas.edu.
D Cole StevensDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA. adriankc@utexas.edu.
M Rachel MehaffeyDepartment of Chemistry, The University of Texas at Austin, Austin, Texas, USA.
Hannah R ManionDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA. adriankc@utexas.edu.
Richard E TaylorDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, Texas, USA.
Adrian T Keatinge-ClayDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA. adriankc@utexas.edu.
The University of Texas at Austin · USUniversity of Notre Dame · US

Funding

Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

C-methyltransferases (MTs) from modular polyketide synthase assembly lines are relatively rare and unexplored domains that are responsible for installing α-methyl groups into nascent polyketide backbones. The stage at which these synthase-embedded enzymes operate during polyketide biosynthesis has yet to be conclusively demonstrated. In this work we establish the activity and substrate preference for six MTs from the gephyronic acid polyketide synthase and demonstrate their ability to methylate both N-acetylcysteamine- and acyl carrier protein-linked β-ketoacylthioester substrates but not malonyl thioester equivalents. These data strongly indicate that MT-catalyzed methylation occurs immediately downstream of ketosynthase-mediated condensation during polyketide assembly. This work represents the first successful report of MT-catalyzed mono- and dimethylation of simple thioester substrates and provides the groundwork for future mechanistic and engineering studies on this important but poorly understood enzymatic domain.

Indexed as

BiocatalysisFatty Acids, MonounsaturatedMethylationMolecular ConformationMyxococcalesPolyketide SynthasesFatty Acids, Monounsaturatedgephyronic acidPolyketide Synthases

Identifiers

PMID27346052
PMCPMC4948183
OpenAlexW2465125219

What OpenQuestion holds

Textmetadata
LicenceTDM
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.