ArticleScientific reports2017
Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 36 citations in OpenAlex.
- Comparative Genomics and Phylogenomics of Novel Radiation-Resistant BacteriumMicroorganisms · 2025Article
- A Novel Thermo-Alkaline Stable GDSL/SGNH Esterase with Broad Substrate Specificity from a Deep-Sea Pseudomonas sp.Marine biotechnology (New York, N.Y.) · 2024Article
- Microbiology and Biochemistry of Pesticides Biodegradation.International journal of molecular sciences · 2023Review
- 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
- Expression, characterization, and immobilization of a novel SGNH esterase Est882 and its potential for pyrethroid degradation.Frontiers in microbiology · 2022Article
- Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S.Scientific reports · 2018Article
- Compartmentalization of the Carbaryl Degradation Pathway: Molecular Characterization of Inducible Periplasmic Carbaryl Hydrolase from Pseudomonas spp.Applied and environmental microbiology · 2018Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The EstPS1 gene, which encodes a novel carboxylesterase of Pseudomonas synxantha PS1 isolated from oil well-produced water, was cloned and sequenced. EstPS1 has an open reading frame of 1923 bp and encodes the 640-amino acid carboxylesterase (EstPS1), which contains an autotransporter (AT) domain (357-640 amino acids). Homology analysis revealed that EstPS1 shared the highest identity (88%) with EstA from Pseudomonas fluorescens A506 (NCBI database) and belonged to the carboxylesterase family (EC 3.1.1.1). The optimum pH and temperature of recombinant EstPS1 were found to be 8.0 and 60 °C, respectively. EstPS1 showed high thermostability, and the half-lives (T
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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.