ArticleComputational and structural biotechnology journal2021
Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Co-expression, purification, and characterization of an acidophilic and n-hexane-tolerant lipase with its foldase from Burkholderia gladioli Bsp-1.Applied microbiology and biotechnology · 2026Article
- Enzymatic characterization and polyurethane biodegradation assay of two novel esterases isolated from a polluted river.PloS one · 2025Article
- Crystallization and preliminary X-ray crystallographic studies of AfeH from Acimetobacter sp. DL-2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica.Extremophiles : life under extreme conditions · 2024Article
- AMWEst, a new thermostable and detergent-tolerant esterase retrieved from the Albian aquifer.Applied microbiology and biotechnology · 2024Article
- Enzymatic Characterization of a Novel HSL Family IV Esterase EstD04 fromMolecules (Basel, Switzerland) · 2023Article
- Thermophilic Carboxylesterases from Hydrothermal Vents of the Volcanic Island of Ischia Active on Synthetic and Biobased Polymers and Mycotoxins.Applied and environmental microbiology · 2023Article
- Whole-Genome Sequencing of a Potential Ester-Synthesizing Bacterium Isolated from Fermented Golden Pomfret and Identification of Its Lipase Encoding Genes.Foods (Basel, Switzerland) · 2022Article
- Bioprospecting for Thermozymes and Characterization of a Novel Lipolytic Thermozyme Belonging to the SGNH/GDSL Family of Hydrolases.International journal of molecular sciences · 2022Article
- Reactivity of a Recombinant Esterase fromMicroorganisms · 2022Article
- Evaluation of a Thermophilic, Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase.Marine drugs · 2022Article
- Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic BacteriumBiomolecules · 2021Article
- Enhanced Production of (S)-2-arylpropionic Acids by Protein Engineering and Whole-Cell Catalysis.Frontiers in bioengineering and biotechnology · 2021Article
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15 authors.
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Abstract
A novel esterase, EstD11, has been discovered in a hot spring metagenomic library. It is a thermophilic and thermostable esterase with an optimum temperature of 60°C. A detailed substrate preference analysis of EstD11 was done using a library of chromogenic ester substrate that revealed the broad substrate specificity of EstD11 with significant measurable activity against 16 substrates with varied chain length, steric hindrance, aromaticity and flexibility of the linker between the carboxyl and the alcohol moiety of the ester. The tridimensional structures of EstD11 and the inactive mutant have been determined at atomic resolutions. Structural and bioinformatic analysis, confirm that EstD11 belongs to the family IV, the hormone-sensitive lipase (HSL) family, from the α/β-hydrolase superfamily. The canonical α/β-hydrolase domain is completed by a cap domain, composed by two subdomains that can unmask of the active site to allow the substrate to enter. Eight crystallographic complexes were solved with different substrates and reaction products that allowed identification of the hot-spots in the active site underlying the specificity of the protein. Crystallization and/or incubation of EstD11 at high temperature provided unique information on cap dynamics and a first glimpse of enzymatic activity
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