ArticleApplied and environmental microbiology2012
Cloning of a novel arylamidase gene from Paracoccus sp. strain FLN-7 that hydrolyzes amide pesticides.
Article in Applied and environmental microbiology, 2012. 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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15 citing papers in PubMed, 63 citations in OpenAlex.
- Functional Characterization and Catalytic Mechanism of an Amidase Involved in Acetaminophen Degradation from Acinetobacter sp.Journal of agricultural and food chemistry · 2026Article
- Article
- Machine Learning Reveals Signatures of Promiscuous Microbial Amidases for Micropollutant Biotransformations.ACS environmental Au · 2025Article
- Identification, characterization, and distribution of novel amidase geneApplied and environmental microbiology · 2024Article
- Characterization of a novel amidohydrolase with promiscuous esterase activity from a soil metagenomic library and its application in degradation of amide herbicides.Environmental science and pollution research international · 2024Article
- Wide substrate range for a candidate bioremediation enzyme isolated from Nocardioides sp. strain SG-4 G.FEMS microbiology letters · 2023Article
- Microbial paracetamol degradation involves a high diversity of novel amidase enzyme candidates.Water research X · 2022Article
- Pollutant Degrading Enzyme: Catalytic Mechanisms and Their Expanded Applications.Molecules (Basel, Switzerland) · 2021Review
- Anaerobic Degradation of Propanil in Soil and Sediment Using Mixed Bacterial Culture.Current microbiology · 2021Article
- Mineralization of the herbicide swep by a two-strain consortium and characterization of a new amidase for hydrolyzing swep.Microbial cell factories · 2020Article
- Microbial degradation of organophosphorus pesticides: novel degraders, kinetics, functional genes, and genotoxicity assessment.Environmental science and pollution research international · 2019Article
- Degradation of Recalcitrant Polyurethane and Xenobiotic Additives by a Selected Landfill Microbial Community and Its Biodegradative Potential Revealed by Proximity Ligation-Based Metagenomic Analysis.Frontiers in microbiology · 2019Article
- An Amidase Gene,Applied and environmental microbiology · 2018Article
- Biodegradation of Pendimethalin by Paracoccus sp. P13.Current microbiology · 2018Article
- Purification and properties of a novel quizalofop-p-ethyl-hydrolyzing esterase involved in quizalofop-p-ethyl degradation by Pseudomonas sp. J-2.Microbial cell factories · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial isolate Paracoccus sp. strain FLN-7 hydrolyzes amide pesticides such as diflubenzuron, propanil, chlorpropham, and dimethoate through amide bond cleavage. A gene, ampA, encoding a novel arylamidase that catalyzes the amide bond cleavage in the amide pesticides was cloned from the strain. ampA contains a 1,395-bp open reading frame that encodes a 465-amino-acid protein. AmpA was expressed in Escherichia coli BL21 and homogenously purified using Ni-nitrilotriacetic acid affinity chromatography. AmpA is a homodimer with an isoelectric point of 5.4. AmpA displays maximum enzymatic activity at 40°C and a pH of between 7.5 and 8.0, and it is very stable at pHs ranging from 5.5 to 10.0 and at temperatures up to 50°C. AmpA efficiently hydrolyzes a variety of secondary amine compounds such as propanil, 4-acetaminophenol, propham, chlorpropham, dimethoate, and omethoate. The most suitable substrate is propanil, with K(m) and k(cat) values of 29.5 μM and 49.2 s(-1), respectively. The benzoylurea insecticides (diflubenzuron and hexaflumuron) are also hydrolyzed but at low efficiencies. No cofactor is needed for the hydrolysis activity. AmpA shares low identities with reported arylamidases (less than 23%), forms a distinct lineage from closely related arylamidases in the phylogenetic tree, and has different biochemical characteristics and catalytic kinetics with related arylamidases. The results in the present study suggest that AmpA is a good candidate for the study of the mechanism for amide pesticide hydrolysis, genetic engineering of amide herbicide-resistant crops, and bioremediation of amide pesticide-contaminated environments.
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