Evidence map›Paper›PMID 36265649›Full record

ArticleArchives of biochemistry and biophysics2022

The Y430F mutant of Salmonella d-ornithine/d-lysine decarboxylase has altered stereospecificity and a putrescine allosteric activation site.

Robert S Phillips, Kim-Ngoc Nguyen Hoang

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

Article in Archives of biochemistry and biophysics, 2022. 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
0.3field-weighted citation impact, top 47% 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, 3 citations in OpenAlex.

  1. Article
  2. Ornithine racemase uses a catalytic cysteine.Biochimica et biophysica acta. Proteins and proteomics · 2026
    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

2 authors at 1 institution in 1 country.

Robert S PhillipsDepartment of Chemistry, University of Georgia, Athens, GA, 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA. Electronic address: plp@uga.edu.
Kim-Ngoc Nguyen HoangDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA.
University of Georgia · US

Funding

Structural and proton dynamics of pyridoxal-5’-phosphate dependent enzymes Resubmission (Equipment Supplement)R01GM137008 · NIGMS · UNIVERSITY OF GEORGIA · PI KOVALEVSKYI, ANDRII Y, MUELLER, LEONARD J · 2020 to 2023
$2.8M
Phase II SER-CAT Optimization: Acquisition of a next generation area detectorS10RR028976 · NCRR · UNIVERSITY OF GEORGIA · PI WANG, BI-CHENG · 2010 to 2010
$1.5M
Acquition of a microdiffractometer for SER-CATS10RR025528 · NCRR · UNIVERSITY OF GEORGIA · PI ROSE, JOHN PATRICK · 2009 to 2009
$414k
Acquisition of an X-ray Generator/Detector System to Support NIH ResearchS10OD021762 · OD · UNIVERSITY OF GEORGIA · PI ROSE, JOHN PATRICK · 2016 to 2016
$412k
NCRR NIH HHS S10 RR025528NCRR NIH HHS S10 RR028976NIGMS NIH HHS R01 GM137008NIH HHS S10 OD021762
6 · The paper itself

Abstract

Tyrosine-430 of d-ornithine/d-lysine decarboxylase (DOKDC) is located in the active site, and was suggested to be responsible for the D-stereospecificity of the enzyme. We have prepared the Y430F mutant form of Salmonella enterica serovar typhimurium DOKDC and evaluated its catalytic activity with D- and l-lysine and ornithine. The kinetic results show that the Y430F mutant has measurable decarboxylase activity with both D- and l-lysine and ornithine, which wild type DOKDC does not. Spectroscopic experiments show that these amino acids bind to form external aldimine complexes with the pyridoxal-5'-phosphate with λ

Indexed as

Carboxy-LyasesOrnithineAllosteric RegulationKineticsLysineMutagenesis, Site-DirectedOrnithine DecarboxylasePutrescinePyridoxal PhosphateSalmonellaCarboxy-LyasesLysinelysine decarboxylaseOrnithineOrnithine DecarboxylasePutrescinePyridoxal PhosphateAllosteric product activationCrystal structureDecarboxylation mechanismStereospecificity

Identifiers

PMID36265649
PMCPMC10351609
OpenAlexW4306678347

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.