ReviewBiochimica et biophysica acta2013
Catalytic mechanisms for phosphotriesterases.
Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 246 citations in OpenAlex.
- Phosphoester hydrolysis using a de novo designed protein: A combined experimental and computational study.Journal of inorganic biochemistry · 2026Article
- Catalytic pBiochemistry · 2026Article
- 3D Bioprinted Engineered Living Microreactors for Continuous Organophosphorus Compound Degradation.Small science · 2025Article
- Broad Substrate Specificity and High Catalytic Activity ofACS omega · 2025Article
- Role of Php domain and related enzymes in the enzymatic degradation of G-series nerve agents.Molecular genetics and genomics : MGG · 2025Review
- A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.Chembiochem : a European journal of chemical biology · 2025Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
- Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.JACS Au · 2024Article
- Applications of Microbial Organophosphate-Degrading Enzymes to Detoxification of Organophosphorous Compounds for Medical Countermeasures against Poisoning and Environmental Remediation.International journal of molecular sciences · 2024Review
- Review
- Improving stereoselectivity of phosphotriesterase (PTE) for kinetic resolution of chiral phosphates.Frontiers in bioengineering and biotechnology · 2024Article
- Warfare Nerve Agents and Paraoxonase-1 as a Potential Prophylactic Therapy against Intoxication.Protein and peptide letters · 2024Review
- Engineering Enzymes for Environmental Sustainability.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Review
- Engineering Enzymes for Environmental Sustainability.Angewandte Chemie (International ed. in English) · 2023Review
- The impact of molecular variants, crystallization conditions and the space group on ligand-protein complexes: a case study on bacterial phosphotriesterase.Acta crystallographica. Section D, Structural biology · 2023Article
- Unusual Relationship between Iron Deprivation and Organophosphate Hydrolase Expression.Applied and environmental microbiology · 2023Article
- Different Strategies Affect Enzyme Packaging into Bacterial Outer Membrane Vesicles.Bioengineering (Basel, Switzerland) · 2023Article
- Ultrahigh-Throughput Directed Evolution of a Metal-Free α/β-Hydrolase with a Cys-His-Asp Triad into an Efficient Phosphotriesterase.Journal of the American Chemical Society · 2023Article
- Degradation insight of organophosphate pesticide chlorpyrifos through novel intermediate 2,6-dihydroxypyridine by Arthrobacter sp. HM01.Bioresources and bioprocessing · 2022Article
- Disposable Paper-Based Biosensors for the Point-of-Care Detection of Hazardous Contaminations-A Review.Biosensors · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Phosphotriesters are one class of highly toxic synthetic compounds known as organophosphates. Wide spread usage of organophosphates as insecticides as well as nerve agents has lead to numerous efforts to identify enzymes capable of detoxifying them. A wide array of enzymes has been found to have phosphotriesterase activity including phosphotriesterase (PTE), methyl parathion hydrolase (MPH), organophosphorus acid anhydrolase (OPAA), diisopropylfluorophosphatase (DFP), and paraoxonase 1 (PON1). These enzymes differ widely in protein sequence and three-dimensional structure, as well as in catalytic mechanism, but they also share several common features. All of the enzymes identified as phosphotriesterases are metal-dependent hydrolases that contain a hydrophobic active site with three discrete binding pockets to accommodate the substrate ester groups. Activation of the substrate phosphorus center is achieved by a direct interaction between the phosphoryl oxygen and a divalent metal in the active site. The mechanistic details of the hydrolytic reaction differ among the various enzymes with both direct attack of a hydroxide as well as covalent catalysis being found. This article is part of a Special Issue entitled: Chemistry and mechanism of phosphatases, diesterases and triesterases.
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Registered trials
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.