Evidence map›Paper›PMID 27158836›Full record

ArticleBiochemistry2016

The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide.

Nathan A Bruender, Vahe Bandarian

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Review
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  10. ACS chemical biology · 2022
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  13. RadicalJournal of the American Chemical Society · 2022
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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

2 authors.

Nathan A BruenderDepartment of Chemistry, University of Utah , Salt Lake City, Utah 84112, United States.
Vahe BandarianDepartment of Chemistry, University of Utah , Salt Lake City, Utah 84112, United States.

Funding

Biosynthesis of Deazapurine-Containing MetabolitesR01GM072623 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2005 to 2017
$3.9M
Mechanistic studies of thioether crosslink formation in peptidesR01GM120638 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2016 to 2017
$695k
NIGMS NIH HHS R01 GM072623NIGMS NIH HHS R01 GM120638
6 · The paper itself

Abstract

Ribosomally synthesized post-translationally modified peptides (RiPPs) are encoded in the genomes of a wide variety of microorganisms, in the proximity of open reading frames that encode enzymes that conduct extensive modifications, many of which are novel. Recently, members of the radical S-adenosyl-l-methionine (SAM) superfamily have been identified in these biosynthetic clusters. Herein, we demonstrate the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. The reaction catalyzed by MftC expands the repertoire of peptide-based radical SAM chemistry beyond the intramolecular cross-links.

Indexed as

Adenosylmethionine DecarboxylaseBacterial ProteinsMycobacterium smegmatisOxidation-ReductionPeptidesAdenosylmethionine DecarboxylaseBacterial ProteinsPeptides

Identifiers

PMID27158836
PMCPMC5331333

What OpenQuestion holds

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Registered trials

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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.