Evidence map›Paper›PMID 31046245›Full record

ArticleBiochemistry2019

Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues.

Paul F Fitzpatrick, Vi Dougherty, Bishnu Subedi, Jesus Quilantan, Cynthia S Hinck, Andreina I Lujan, Jose R Tormos

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

Article in Biochemistry, 2019. 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, top 97% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  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

7 authors at 2 institutions in 1 country.

Paul F FitzpatrickDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.ORCID 0000-0002-8486-2024
Vi DoughertyDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.
Bishnu SubediDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.
Jesus QuilantanDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.
Cynthia S HinckDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.
Andreina I LujanDepartment of Biochemistry and Structural Biology , University of Texas Health Science Center , San Antonio , Texas 78229 , United States.
Jose R TormosDepartment of Chemistry , St. Mary's University , San Antonio , Texas 78228 , United States.
The University of Texas Health Science Center at San Antonio · USSt. Mary's University, Texas · 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 d-6-hydroxynicotine oxidase catalyzes an early step in the oxidation of ( R)-nicotine, the oxidation of a carbon-nitrogen bond in the pyrrolidine ring of ( R)-6-hydroxynicotine. The enzyme is a member of the vanillyl alcohol oxidase/ p-cresol methylhydroxylase family of flavoproteins. The effects of substrate modifications on the steady-state and rapid-reaction kinetic parameters are not consistent with the quinone-methide mechanism of p-cresol methylhydroxylase. There is no solvent isotope effect on the k

Indexed as

BiocatalysisCatalytic DomainEscherichia coliHydrogen BondingHydrogen-Ion ConcentrationIsotopesKineticsMicrococcaceaeMixed Function OxygenasesNicotineOxidation-ReductionOxidoreductasesPlasmidsSubstrate Specificity4-cresol dehydrogenase (hydroxylating)6-hydroxynicotineIsotopesMixed Function OxygenasesNicotineOxidoreductases

Identifiers

PMID31046245
PMCPMC6786761
OpenAlexW2942929070

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.