Evidence map›Paper›PMID 19615330›Full record

ArticleArchives of biochemistry and biophysics2009

Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.

Renda Hawwa, John Aikens, Robert J Turner, Bernard D Santarsiero, Andrew D Mesecar

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 73 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

5 authors at 3 institutions in 1 country.

Renda HawwaDepartment of Medicinal Chemistry and Pharmacognosy and the Center for Pharmaceutical Biotechnology, University of Illinois at Chicago, Chicago, IL 60607, USA.
John Aikens
Robert J Turner
Bernard D Santarsiero
Andrew D Mesecar
Lybradyn (United States) · USUniversity of Illinois Chicago · USAshland (United States) · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
Novel Organophosphorous Hydrolases for DecontaminationR42GM072357 · NIGMS · LYBRADYN, INC. · PI MESECAR, ANDREW D · 2006 to 2007
$718k
Macromolecular X-ray Structure Facility InstrumentationS10RR017744 · NCRR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MESECAR, ANDREW D · 2003 to 2003
$346k
Novel Organophosphorous Hydrolases for DecontaminationR41GM072357 · NIGMS · LYBRADYN, INC. · PI MESECAR, ANDREW D · 2004 to 2004
$96k
NCRR NIH HHS P41 RR007707NCRR NIH HHS S10 RR017744NIGMS NIH HHS 2 R41 GM072357NIGMS NIH HHS R41 GM072357NIGMS NIH HHS R42 GM072357
6 · The paper itself

Abstract

A new enzyme homologous to phosphotriesterase was identified from the bacterium Geobacillus stearothermophilus (GsP). This enzyme belongs to the amidohydrolase family and possesses the ability to hydrolyze both lactone and organophosphate (OP) compounds, making it a phosphotriesterase-like lactonase (PLL). GsP possesses higher OP-degrading activity than recently characterized PLLs, and it is extremely thermostable. GsP is active up to 100 degrees C with an energy of activation of 8.0 kcal/mol towards ethyl paraoxon, and it can withstand an incubation temperature of 60 degrees C for two days. In an attempt to understand the thermostability of PLLs, the X-ray structure of GsP was determined and compared to those of existing PLLs. Based upon a comparative analysis, a new thermal advantage score and plot was developed and reveals that a number of different factors contribute to the thermostability of PLLs.

Indexed as

TemperatureAmino Acid SequenceBinding SitesCarboxylic Ester HydrolasesCloning, MolecularCrystallizationDimerizationEnzyme StabilityEscherichia coliGenome, BacterialGeobacillus stearothermophilusHydrogen BondingHydrolysisHydrophobic and Hydrophilic InteractionsKineticsModels, ChemicalCarboxylic Ester HydrolasesgluconolactonasePhosphoric Triester Hydrolases

Identifiers

PMID19615330
PMCPMC5433624
OpenAlexW1964575015

What OpenQuestion holds

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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.