Evidence map›Paper›PMID 32531315›Full record

ArticleArchives of biochemistry and biophysics2020

The metal- and substrate-dependences of 2,4'-dihydroxyacetophenone dioxygenase.

Kenneth M Roberts, Gabrielle C Connor, C Haley Cave, Gerard T Rowe, Clinton A Page

Abstract read
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In one paragraph

Article in Archives of biochemistry and biophysics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Kenneth M RobertsDepartment of Chemistry and Physics, University of South Carolina Aiken, Aiken, SC, 29801, USA. Electronic address: KenR@usca.edu.
Gabrielle C ConnorDepartment of Chemistry and Physics, University of South Carolina Aiken, Aiken, SC, 29801, USA. Electronic address: gcconnor@usca.edu.
C Haley CaveDepartment of Chemistry and Physics, University of South Carolina Aiken, Aiken, SC, 29801, USA. Electronic address: ccave@usca.edu.
Gerard T RoweDepartment of Chemistry and Physics, University of South Carolina Aiken, Aiken, SC, 29801, USA. Electronic address: gerardr@usca.edu.
Clinton A PageDepartment of Biology and Geology, University of South Carolina Aiken, Aiken, SC, 29801, USA. Electronic address: clintp@usca.edu.

Funding

South Carolina IDeA Networks of Biomedical Research (SC INBRE V)P20GM103499 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI EDIE C GOLDSMITH · 2012 to 2026
$61.0M
Supplement for South Carolina BRIN - 1P20 RR16461P20RR016461 · NCRR · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI DEAVOR, JAMES · 2001 to 2011
$32.3M
NCRR NIH HHS P20 RR016461NIGMS NIH HHS P20 GM103499
6 · The paper itself

Abstract

While the enzyme, 2,4'-dihydroxyacetophenone dioxygenase (DAD), has been known for decades, very little has been characterized of the mechanism of the DAD-catalyzed oxidative cleavage of its reported substrate, 2,4'-dihydroxyacetophenone (DHA). The purpose of this study was to identify the active metal center and to characterize the substrate-dependence of the kinetics of the reaction to lay the foundation for deeper mechanistic investigation. To this, the DAD V1M mutant (bDAD) was overexpressed, purified, and reconstituted with various metal ions. Kinetic assays evaluating the activity of the reconstituted enzyme as well as the substrate- and product-dependences of the reaction kinetics were performed. The results from reconstitution of the apoprotein with a variety of metal ions support the requirement for an Fe

Indexed as

AcetophenonesBurkholderiaCatalysisDioxygenasesIronKineticsOxidation-Reduction2,4'-dihydroxyacetophenone dioxygenaseAcetophenonesDioxygenasesIron2,4′-dihydroxyacetophenone dioxygenaseDioxygenaseNon-heme ironSteady-state kineticsSubstrate-dependence

Identifiers

PMID32531315
PMCPMC7484352

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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.