Evidence map›Paper›PMID 35588368›Full record

ArticleAngewandte Chemie (International ed. in English)2022

An Unusual Oxidative Rearrangement Catalyzed by a Divergent Member of the 2-Oxoglutarate-Dependent Dioxygenase Superfamily during Biosynthesis of Dehydrofosmidomycin.

Elizabeth I Parkinson, Hani G Lakkis, Amir A Alwali, Mary Elizabeth M Metcalf, Ramya Modi, William W Metcalf

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. LcSAO1, an Unconventional DOXB Clade 2OGD Enzyme fromInternational journal of molecular sciences · 2023
    Article
  3. Review
  4. Review
  5. 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

6 authors at 2 institutions in 1 country.

Elizabeth I ParkinsonInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 W. Gregory Dr., Urbana, IL 61801, USA.ORCID 0000-0002-3665-5522
Hani G LakkisDepartment of Chemistry, Purdue University, Herbert C. Brown Laboratory of Chemistry, Room 4103E, 560 Oval Drive, Box 59, West Lafayette, IN 47907, USA.
Amir A AlwaliDepartment of Chemistry, Purdue University, Herbert C. Brown Laboratory of Chemistry, Room 4103E, 560 Oval Drive, Box 59, West Lafayette, IN 47907, USA.
Mary Elizabeth M MetcalfInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 W. Gregory Dr., Urbana, IL 61801, USA.
Ramya ModiDepartment of Chemistry, Purdue University, Herbert C. Brown Laboratory of Chemistry, Room 4103E, 560 Oval Drive, Box 59, West Lafayette, IN 47907, USA.ORCID 0000-0003-0695-4705
William W MetcalfInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 W. Gregory Dr., Urbana, IL 61801, USA.ORCID 0000-0002-0182-0671
Purdue University West Lafayette · USUniversity of Illinois Urbana-Champaign · US

Funding

Mining Cryptic Biosynthetic Gene Clusters for Novel Bioactive Compounds and BiocatalystsR35GM138002 · NIGMS · PURDUE UNIVERSITY · PI Elizabeth Ivy Parkinson · 2020 to 2026
$2.9M
Discovery, biosynthesis and bioactivity of phosphonic acid natural productsR01GM127659 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI METCALF, WILLIAM W · 2018 to 2024
$2.2M
Request for a Varian 600 MHz NMR InstrumentS10RR028833 · NCRR · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2011 to 2011
$600k
NCRR NIH HHS S10 RR028833NIGMS NIH HHS R01 GM127659NIGMS NIH HHS R35 GM138002
6 · The paper itself

Abstract

The biosynthesis of the natural product dehydrofosmidomycin involves an unusual transformation in which 2-(trimethylamino)ethylphosphonate is rearranged, desaturated and demethylated by the enzyme DfmD, a divergent member of the 2-oxoglutarate-dependent dioxygenase superfamily. Although other members of this enzyme family catalyze superficially similar transformations, the combination of all three reactions in a single enzyme has not previously been observed. By characterizing the products of in vitro reactions with labeled and unlabeled substrates, we show that DfmD performs this transformation in two steps, with the first involving desaturation of the substrate to form 2-(trimethylamino)vinylphosphonate, and the second involving rearrangement and demethylation to form methyldehydrofosmidomycin. These data reveal significant differences from the desaturation and rearrangement reactions catalyzed by other family members.

Indexed as

DioxygenasesKetoglutaric AcidsCatalysisOxidation-ReductionOxidative StressDioxygenasesKetoglutaric AcidsBiosynthesisEnzyme CatalysisNatural ProductsPhosphonates

Identifiers

PMID35588368
PMCPMC9296572
OpenAlexW4280509289

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.