ArticlePloS one2013
Molecular cloning and characterization of a newly isolated pyrethroid-degrading esterase gene from a genomic library of Ochrobactrum anthropi YZ-1.
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 10 papers.
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Who cites it
10 citing papers in PubMed.
- Optimizing microbial strain selection for pyrethroid biodegradation in contaminated environments through a TOPSIS-based decision-making system.Scientific reports · 2024Article
- Microbial elimination of pyrethroids: specific strains and involved enzymes.Applied microbiology and biotechnology · 2022Review
- Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation.Frontiers in microbiology · 2022Article
- Highly efficient degradation of cypermethrin by a co-culture ofFrontiers in microbiology · 2022Article
- Pyrethroid Carboxylesterase PytH fromApplied and environmental microbiology · 2020Article
- Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S.Scientific reports · 2018Article
- Identification and immobilization of a novel cold-adapted esterase, and its potential for bioremediation of pyrethroid-contaminated vegetables.Microbial cell factories · 2017Article
- Directed evolution and secretory expression of a pyrethroid-hydrolyzing esterase with enhanced catalytic activity and thermostability.Microbial cell factories · 2017Article
- Bacterial Expression and Kinetic Analysis of Carboxylesterase 001D from Helicoverpa armigera.International journal of molecular sciences · 2016Article
- Pyrethroid-Degrading Microorganisms and Their Potential for the Bioremediation of Contaminated Soils: A Review.Frontiers in microbiology · 2016Review
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7 authors.
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Abstract
A novel pyrethroid-degrading esterase gene pytY was isolated from the genomic library of Ochrobactrum anthropi YZ-1. It possesses an open reading frame (ORF) of 897 bp. Blast search showed that its deduced amino acid sequence shares moderate identities (30% to 46%) with most homologous esterases. Phylogenetic analysis revealed that PytY is a member of the esterase VI family. pytY showed very low sequence similarity compared with reported pyrethroid-degrading genes. PytY was expressed, purified, and characterized. Enzyme assay revealed that PytY is a broad-spectrum degrading enzyme that can degrade various pyrethroids. It is a new pyrethroid-degrading gene and enriches genetic resource. Kinetic constants of Km and Vmax were 2.34 mmol·L(-1) and 56.33 nmol min(-1), respectively, with lambda-cyhalothrin as substrate. PytY displayed good degrading ability and stability over a broad range of temperature and pH. The optimal temperature and pH were of 35°C and 7.5. No cofactors were required for enzyme activity. The results highlighted the potential use of PytY in the elimination of pyrethroid residuals from contaminated environments.
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