Evidence map›Paper›PMID 23049981›Full record

ArticlePloS one2012

Phenylalanine hydroxylase from Legionella pneumophila is a thermostable enzyme with a major functional role in pyomelanin synthesis.

Marte I Flydal, Christa H Chatfield, Huaixin Zheng, Felizza F Gunderson, Oscar Aubi, Nicholas P Cianciotto, Aurora Martinez

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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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 2 countries.

Marte I FlydalDepartment of Biomedicine, University of Bergen, Bergen, Norway.
Christa H Chatfield
Huaixin Zheng
Felizza F Gunderson
Oscar Aubi
Nicholas P Cianciotto
Aurora Martinez
Northwestern University · USUniversity of Bergen · NO

Funding

TRAINING PROGRAM IN IMMUNOLOGY &MOLECULAR PATHOGENESIST32AI007476 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Edward Benjamin Thorp · 1996 to 2026
$6.6M
GENETICS OF IRON ACQUISITION BY LEGIONELLA PNEUMOPHILAR01AI034937 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 1995 to 2014
$4.5M
Pyomelanin and Legionella pneumophila InfectionR21AI089712 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 2010 to 2011
$417k
NIAID NIH HHS AI034937NIAID NIH HHS AI089712NIAID NIH HHS R01 AI034937NIAID NIH HHS R21 AI089712NIAID NIH HHS T32 AI0007476NIAID NIH HHS T32 AI007476
6 · The paper itself

Abstract

backgroundLegionella pneumophila is a pathogenic bacterium that can cause Legionnaires' disease and other non-pneumonic infections in humans. This bacterium produces a pyomelanin pigment, a potential virulence factor with ferric reductase activity. In this work, we have investigated the role of phenylalanine hydroxylase from L. pneumophila (lpPAH), the product of the phhA gene, in the synthesis of the pyomelanin pigment and the growth of the bacterium in defined compositions. METHODOLOGY/PRINCIPAL

findingsComparative studies of wild-type and phhA mutant corroborate that lpPAH provides the excess tyrosine for pigment synthesis. phhA and letA (gacA) appear transcriptionally linked when bacteria were grown in buffered yeast extract medium at 37°C. phhA is expressed in L. pneumophila growing in macrophages. We also cloned and characterized lpPAH, which showed many characteristics of other PAHs studied so far, including Fe(II) requirement for activity. However, it also showed many particular properties such as dimerization, a high conformational thermal stability, with a midpoint denaturation temperature (T(m)) = 79 ± 0.5°C, a high specific activity at 37°C (10.2 ± 0.3 µmol L-Tyr/mg/min) and low affinity for the substrate (K(m) (L-Phe) = 735 ± 50 µM. CONCLUSIONS/SIGNIFICANCE: lpPAH has a major functional role in the synthesis of pyomelanin and promotes growth in low-tyrosine media. The high thermal stability of lpPAH might reflect the adaptation of the enzyme to withstand relatively high survival temperatures.

Indexed as

Bacterial ProteinsEnzyme StabilityLegionella pneumophilaMelaninsPhenylalanine HydroxylaseTemperatureTyrosineBacterial ProteinsMelaninsPhenylalanine HydroxylasepyomelaninTyrosine

Identifiers

PMID23049981
PMCPMC3458870
OpenAlexW1985126826

What OpenQuestion holds

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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.