Evidence map›Paper›PMID 39772443›Full record

ArticleJournal of the American Chemical Society2025

Spectroscopic and Computational Insights into the Mechanism of Cofactor Cobalt-Carbon Bond Homolysis by the Adenosylcobalamin-Dependent Enzyme Ethanolamine Ammonia-Lyase.

Laura D Elmendorf, Ryan L Hall, Flavia G Costa, Jorge C Escalante-Semerena, Thomas C Brunold

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

5 authors.

Laura D ElmendorfDepartment of Chemistry, University of Wisconsin─Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States.
Ryan L HallDepartment of Chemistry, University of Wisconsin─Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States.
Flavia G CostaDepartment of Microbiology, University of Georgia─Athens, Cedar Street Building C, Athens, Georgia 30602, United States.ORCID 0000-0001-7058-6009
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia─Athens, Cedar Street Building C, Athens, Georgia 30602, United States.ORCID 0000-0001-7428-2811
Thomas C BrunoldDepartment of Chemistry, University of Wisconsin─Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0001-6516-598X

Funding

Analysis of the Metabolic Capabilities of Prokaryotic CellsR35GM130399 · NIGMS · UNIVERSITY OF GEORGIA · PI JORGE C ESCALANTE · 2019 to 2026
$5.5M
Studies of metal-containing and metal-less EutT adenosyltransferasesF31GM122394 · NIGMS · UNIVERSITY OF GEORGIA · PI COSTA, FLAVIA GISELA · 2017 to 2020
$176k
NIGMS NIH HHS F31 GM122394NIGMS NIH HHS R35 GM130399
6 · The paper itself

Abstract

The adenosylcobalamin (AdoCbl)-dependent enzyme ethanolamine ammonia-lyase (EAL) catalyzes the conversion of ethanolamine to acetaldehyde and ammonia. As is the case for all AdoCbl-dependent isomerases, the catalytic cycle of EAL is initiated by homolytic cleavage of the cofactor's Co-C bond, producing Co

Indexed as

CarbonCobaltCobamidesEthanolamine Ammonia-LyaseDensity Functional TheoryCarbonCobaltcobamamideCobamidesEthanolamine Ammonia-Lyase

Identifiers

PMID39772443
PMCPMC12281503

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.