Evidence map›Paper›PMID 31604072›Full record

ArticleArchives of biochemistry and biophysics2019

pH and deuterium isotope effects on the reaction of trimethylamine dehydrogenase with dimethylamine.

Udayanga S Wanninayake, Bishnu Subedi, Paul F Fitzpatrick

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of biochemistry and biophysics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Review
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

3 authors at 1 institution in 1 country.

Udayanga S WanninayakeDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center, San Antonio, TX, 78229, USA.
Bishnu SubediDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center, San Antonio, TX, 78229, USA.
Paul F FitzpatrickDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center, San Antonio, TX, 78229, USA. Electronic address: fitzpatrickp@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · US

Funding

Mechanisms of FlavoproteinsR01GM058698 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FITZPATRICK, PAUL F. · 1999 to 2017
$4.6M
NIGMS NIH HHS R01 GM058698
6 · The paper itself

Abstract

The flavoprotein trimethylamine dehydrogenase is a member of a small class of flavoproteins that catalyze amine oxidation and transfer the electrons through an Fe/S center to an external oxidant. The mechanism of amine oxidation by this family of enzymes has not been established. Here, we describe the use of pH and kinetic isotope effects with the slow substrate dimethylamine to study the mechanism. The data are consistent with the neutral amine being the form of the substrate that binds productively at the pH optimum, since the pK

Indexed as

BiocatalysisDeuteriumDimethylaminesHydrogen-Ion ConcentrationKineticsMethylophilus methylotrophusOxidoreductases, N-DemethylatingProtein BindingSubstrate SpecificityDeuteriumdimethylamineDimethylaminesOxidoreductases, N-Demethylatingtrimethylamine dehydrogenaseAmine oxidationEnzyme mechanismFlavoproteinIsotope effectpH effectTrimethylamine dehydrogenase

Identifiers

PMID31604072
PMCPMC6924622
OpenAlexW2979298045

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.