Evidence map›Paper›PMID 23851010›Full record

ArticleFEBS letters2013

A mutational analysis of active site residues in trans-3-chloroacrylic acid dehalogenase.

Gerrit J Poelarends, Hector Serrano, Jamison P Huddleston, William H Johnson, Christian P Whitman

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2013. 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
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.

  1. 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

5 authors.

Gerrit J PoelarendsDivision of Medicinal Chemistry, College of Pharmacy, The University of Texas, Austin, TX 78712-1074, USA.
Hector Serrano
Jamison P Huddleston
William H Johnson
Christian P Whitman

Funding

Structure and Mechanism in the Tautomerase SuperfamilyR01GM065324 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI WHITMAN, CHRISTIAN P. · 2002 to 2011
$2.3M
NIGMS NIH HHS GM-65324NIGMS NIH HHS R01 GM065324
6 · The paper itself

Abstract

trans-3-Chloroacrylic acid dehalogenase (CaaD) catalyzes the hydrolytic dehalogenation of trans-3-haloacrylates to yield malonate semialdehyde by a mechanism utilizing βPro-1, αArg-8, αArg-11, and αGlu-52. These residues are implicated in a promiscuous hydratase activity where 2-oxo-3-pentynoate is processed to acetopyruvate. The roles of three nearby residues (βAsn-39, αPhe-39, and αPhe-50) are unexplored. Mutants were constructed at these positions (βN39A, αF39A, αF39T, αF50A and αF50Y) and kinetic parameters determined along with those of the αR8K and αR11K mutants. Analysis indicates that αArg-8, αArg-11, and βAsn-39 are critical for dehalogenase activity whereas αArg-11 and αPhe-50 are critical for hydratase activity. Docking studies suggest structural bases for these observations.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCatalytic DomainHydrogen BondingHydrogen-Ion ConcentrationHydrolasesKineticsMolecular Docking SimulationMolecular WeightMutagenesis, Site-DirectedMutant ProteinsProtein BindingProtein Structure, SecondaryPseudomonasBacterial ProteinsHydrolasesMutant Proteinstrans-3-chloroacrylic acid dehalogenaseEnzyme mechanismHydrolytic dehalogenationTautomerase superfamilytrans-3-Chloroacrylic acid dehalogenase

Identifiers

PMID23851010
PMCPMC3779635

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Registered trials

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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.