ArticlePloS one2013
Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- 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
- Response Surface Methodology Based Optimization, Partial Purification and Characterization of Alkaline Phosphatase Isolated from Pseudomonas asiatica Strain ZKB1 and its Application in Plant Growth Promotion.Molecular biotechnology · 2022Article
- Environmental Distribution, Metabolic Fate, and Degradation Mechanism of Chlorpyrifos: Recent and Future Perspectives.Applied biochemistry and biotechnology · 2022Review
- Environmental Occurrence, Toxicity Concerns, and Degradation of Diazinon Using a Microbial System.Frontiers in microbiology · 2021Review
- Degradation of Acephate and Its Intermediate Methamidophos: Mechanisms and Biochemical Pathways.Frontiers in microbiology · 2020Review
- Organophosphorus Nerve Agents: Types, Toxicity, and Treatments.Journal of toxicology · 2020Review
- AidB, a Novel ThermostableApplied and environmental microbiology · 2019Article
- Signal Disruption Leads to Changes in Bacterial Community Population.Frontiers in microbiology · 2019Article
- Purification and characterization of alkaline phosphatase from lactic acid bacteria.RSC advances · 2018Article
- Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.Scientific reports · 2018Article
- Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes.Environmental science and pollution research international · 2016Review
- Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity.Biochemistry · 2015Article
- Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.Scientific reports · 2015Article
- Prodrugs of phosphonates and phosphates: crossing the membrane barrier.Topics in current chemistry · 2015Review
- SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.BMC research notes · 2014Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundOrganophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-β-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities. PRINCIPAL
findingsThe X-ray structure of OPHC2 has been solved at 2.1 Å resolution. The enzyme is roughly globular exhibiting a αβ/βα topology typical of the metallo-β-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8°C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones. SIGNIFICANCE: OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis.
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