ArticleScientific reports2016
Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- ProteoSeeker: A Feature-Rich Metagenomic Analysis Tool for Accessible and Comprehensive Metagenomic Exploration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- AMWEst, a new thermostable and detergent-tolerant esterase retrieved from the Albian aquifer.Applied microbiology and biotechnology · 2024Article
- Biomimetic COEnvironmental science & technology · 2024Article
- Discovery of Novel Inhibitors against ALS-Related SOD1(A4V) Aggregation through the Screening of a Chemical Library Using Differential Scanning Fluorimetry (DSF).Pharmaceuticals (Basel, Switzerland) · 2024Article
- Nanobiocatalysts with inbuilt cofactor recycling for oxidoreductase catalysis in organic solvents.Nanoscale advances · 2023Article
- Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.Microorganisms · 2022Article
- Finding Superior Biocatalysts via Homolog Screening.Chem catalysis · 2022Article
- Metagenomic Screening for Lipolytic Genes Reveals an Ecology-Clustered Distribution Pattern.Frontiers in microbiology · 2022Article
- Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family.Frontiers in microbiology · 2022Article
- Characterization of a novel thermostable alkaline lipase derived from a compost metagenomic library and its potential application in the detergent industry.Frontiers in microbiology · 2022Article
- Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24.Extremophiles : life under extreme conditions · 2021Article
- Cloning, heterologous expression, and characterization of a novel thioesterase from natural sample.Heliyon · 2021Article
- Bioprospecting of Novel Extremozymes From Prokaryotes-The Advent of Culture-Independent Methods.Frontiers in microbiology · 2021Review
- Biochemical characterization of an esterase from Clostridium acetobutylicum with novel GYSMG pentapeptide motif at the catalytic domain.Journal of industrial microbiology & biotechnology · 2020Article
- XynDZ5: A New Thermostable GH10 Xylanase.Frontiers in microbiology · 2020Article
- Multidisciplinary involvement and potential of thermophiles.Folia microbiologica · 2019Review
- A hydrolase with esterase activity expressed from a fosmid gene bank prepared from DNA of a North West Himalayan glacier frozen soil sample.3 Biotech · 2019Article
- Metagenome-assembled genomes provide new insight into the microbial diversity of two thermal pools in Kamchatka, Russia.Scientific reports · 2019Article
- ANASTASIA: An Automated Metagenomic Analysis Pipeline for Novel Enzyme Discovery Exploiting Next Generation Sequencing Data.Frontiers in genetics · 2019Article
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9 authors.
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Abstract
Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Here, we have identified a new esterolytic enzyme by screening a metagenomic sample collected from a hot spring in Kamchatka, Russia. Biochemical characterization of the new esterase, termed EstDZ2, revealed that it is highly active against medium chain fatty acid esters at temperatures between 25 and 60 °C and at pH values 7-8. The new enzyme is moderately thermostable with a half-life of more than six hours at 60 °C, but exhibits exquisite stability against high concentrations of organic solvents. Phylogenetic analysis indicated that EstDZ2 is likely an Acetothermia enzyme that belongs to a new family of bacterial esterases, for which we propose the index XV. One distinctive feature of this new family, is the presence of a conserved GHSAG catalytic motif. Multiple sequence alignment, coupled with computational modelling of the three-dimensional structure of EstDZ2, revealed that the enzyme lacks the largest part of the "cap" domain, whose extended structure is characteristic for the closely related Family IV esterases. Thus, EstDZ2 appears to be distinct from known related esterolytic enzymes, both in terms of sequence characteristics, as well as in terms of three-dimensional structure.
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