Evidence map›Paper›PMID 29986514›Full record

ArticleMolecules (Basel, Switzerland)2018

Theoretical Studies on Catalysis Mechanisms of Serum Paraoxonase 1 and Phosphotriesterase Diisopropyl Fluorophosphatase Suggest the Alteration of Substrate Preference from Paraoxonase to DFP.

Hao Zhang, Ling Yang, Ying-Ying Ma, Chaoyuan Zhu, Shenghsien Lin, Rong-Zhen Liao

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

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Evolutionary insights into the active-site structures of the metallo-β-lactamase superfamily from a classification study with support vector machine.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  4. 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

6 authors at 5 institutions in 2 countries.

Hao ZhangCollege of Life Science and Engineering, Northwest Minzu University, Lanzhou 730030, China. zhang_hao@mail.bnu.edu.cn.ORCID 0000-0001-7752-1769
Ling YangMIIT Key Laboratory of Critical Materials Technology for New Energy Conversion and Storage, School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin 150001, China. yangling@hit.edu.cn.ORCID 0000-0002-5635-2860
Ying-Ying MaInner Mongolia University of Technology, Hohhot 010051, China. yyma@imut.edu.cn.
Chaoyuan ZhuDepartment of Applied Chemistry, Institute of Molecular Science and Center for Interdisciplinary Molecular Science, National Chiao-Tung University, Hsinchu 30050, Taiwan. cyzhu@mail.nctu.edu.tw.
Shenghsien LinDepartment of Applied Chemistry, Institute of Molecular Science and Center for Interdisciplinary Molecular Science, National Chiao-Tung University, Hsinchu 30050, Taiwan. sheng@mail.nctu.edu.tw.
Rong-Zhen LiaoKey Laboratory for Large-Format Battery Materials and System, Ministry of Education School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan 430074, China. rongzhen@hust.edu.cn.
National Yang Ming Chiao Tung University · TWHarbin Institute of Technology · CNHuazhong University of Science and Technology · CNInner Mongolia University of Technology · CNMinzu University of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The calcium-dependent β-propeller proteins mammalian serum paraoxonase 1 (PON1) and phosphotriesterase diisopropyl fluorophosphatase (DFPase) catalyze the hydrolysis of organophosphorus compounds and enhance hydrolysis of various nerve agents. In the present work, the phosphotriesterase activity development between PON1 and DFPase was investigated by using the hybrid density functional theory method B3LYP. Based on the active-site difference between PON1 and DFPase, both the wild type and the mutant (a water molecule replacing Asn270 in PON1) models were designed. The results indicated that the substitution of a water molecule for Asn270 in PON1 had little effect on the enzyme activity in kinetics, while being more efficient in thermodynamics, which is essential for DFP hydrolysis. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca

Indexed as

AnimalsAryldialkylphosphataseBiocatalysisCalciumCatalytic DomainEvolution, MolecularHumansHydrogen BondingMammalsMutationOrganophosphorus CompoundsPhosphoric Triester HydrolasesProtein ConformationThermodynamicsAryldialkylphosphataseCalciumdiisopropyl-fluorophosphataseOrganophosphorus CompoundsPhosphoric Triester Hydrolasesenzyme evolutionhydrolysisplasticityreaction mechanismβ-propeller protein

Identifiers

PMID29986514
PMCPMC6100192
OpenAlexW2840955542

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.