ArticleScientific reports2018
Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 50 citations in OpenAlex.
- Elucidating the kinetics and mechanisms of tetramethrin biodegradation by the fungal strain Neocosmospora sp. AF3.Microbial cell factories · 2025Article
- Microbes' role in environmental pollution and remediation: a bioeconomy focus approach.AIMS microbiology · 2024Review
- Microbial elimination of pyrethroids: specific strains and involved enzymes.Applied microbiology and biotechnology · 2022Review
- Whole genome sequencing and analysis of fenvalerate degrading bacteria Citrobacter freundii CD-9.AMB Express · 2022Article
- Characteristics and Application ofFrontiers in bioengineering and biotechnology · 2022Review
- Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation.Frontiers in microbiology · 2022Article
- Bioremediation of Agricultural Soils Polluted with Pesticides: A Review.Bioengineering (Basel, Switzerland) · 2021Review
- Insight Into Microbial Applications for the Biodegradation of Pyrethroid Insecticides.Frontiers in microbiology · 2019Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30-46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a Km and Vmax value of 0.734 ± 0.013 mmol·l
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