ArticleThe Biochemical journal1998
Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 143 citations in OpenAlex.
- Cloning and Characterization of GDSL Esterases fromBiology · 2026Article
- Advances and Challenges in the Development of Immobilized Enzymes for Batch and Flow Biocatalyzed Processes.ChemSusChem · 2025Review
- Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica.Extremophiles : life under extreme conditions · 2024Article
- Computational analysis of carboxylesterase genes and proteins in non-pathogenic food bacterium Alicyclobacillus acidocaldarius: insights from proteogenomics.World journal of microbiology & biotechnology · 2023Article
- Development of a Qualitative Test to Detect the Presence of Organophosphate Pesticides on Fruits and Vegetables.Life (Basel, Switzerland) · 2023Article
- Monitoring of pesticide amount in water and drinkable food by a fluorescence-based biosensor.EFSA journal. European Food Safety Authority · 2022Article
- Reactivity of a Recombinant Esterase fromMicroorganisms · 2022Article
- MOF-Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents.Angewandte Chemie (International ed. in English) · 2022Article
- A 3D printable adapter for solid-state fluorescence measurements: the case of an immobilized enzymatic bioreceptor for organophosphate pesticides detection.Analytical and bioanalytical chemistry · 2022Article
- A FRET Approach to Detect Paraoxon among Organophosphate Pesticides Using a Fluorescent Biosensor.Sensors (Basel, Switzerland) · 2022Article
- Systematic evaluation of agarose- and agar-based bioinks for extrusion-based bioprinting of enzymatically active hydrogels.Frontiers in bioengineering and biotechnology · 2022Article
- Characterization of a novel halotolerant esterase from3 Biotech · 2020Article
- Highly Sensitive Detection of Chemically Modified Thio-Organophosphates by an Enzymatic Biosensing Device: An Automated Robotic Approach.Sensors (Basel, Switzerland) · 2020Article
- Determination of Picomolar Concentrations of Paraoxon in Human Urine by Fluorescence-Based Enzymatic Assay.Sensors (Basel, Switzerland) · 2019Article
- Innovative Biocatalysts as Tools to Detect and Inactivate Nerve Agents.Scientific reports · 2018Article
- Development of an automated multienzymatic biosensor for risk assessment of pesticide contamination in water and food.EFSA journal. European Food Safety Authority · 2018Article
- Structural features determining thermal adaptation of esterases.Protein engineering, design & selection : PEDS · 2016Article
- Enlarging the substrate portfolio of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius.Extremophiles : life under extreme conditions · 2015Article
- Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family.The Journal of biological chemistry · 2015Article
- Fluorescence spectroscopy approaches for the development of a real-time organophosphate detection system using an enzymatic sensor.Sensors (Basel, Switzerland) · 2015Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously purified a new esterase from the thermoacidophilic eubacterium Bacillus acidocaldarius whose N-terminal sequence corresponds to an open reading frame (ORF3) reported to show homology with the mammalian hormone-sensitive lipase (HSL)-like group of the esterase/lipase family. To compare the biochemical properties of this thermophilic enzyme with those of the homologous mesophilic and psychrophilic members of the HSL group, an overexpression system in Escherichia coli was established. The protein, expressed in soluble and active form at 10 mg/l E. coli culture, was purified to homogeneity and characterized biochemically. The enzyme, a 34 kDa monomeric protein, was demonstrated to be a B'-type carboxylesterase (EC 3.1.1.1) on the basis of substrate specificity and the action of inhibitors. Among the p-nitrophenyl (PNP) esters tested the best substrate was PNP-exanoate with Km and kcat values of 11+/-2 microM (mean+/-S.D., n=3) and 6610+/-880 s-1 (mean+/-S.D., n=3) respectively at 70 degreesC and pH7.1. In spite of relatively high sequence identity with the mammalian HSLs, the psychrophilic Moraxella TA144 lipase 2 and the human liver arylacetamide deacetylase, no lipase or amidase activity was detected. A series of substrates were tested for enantioselectivity. Substantial enantioselectivity was observed only in the resolution of (+/-)-3-bromo-5-(hydroxymethyl)-Delta2-isoxazoline, where the (R)-product was obtained with an 84% enantiomeric excess at 36% conversion. The enzyme was also able to synthesize acetyl esters when tested in vinyl acetate and toluene. Inactivation by diethylpyrocarbonate, diethyl-p-nitrophenyl phosphate, di-isopropylphosphofluoridate (DFP) and physostigmine, as well as labelling with [3H]DFP, supported our previous suggestion of a catalytic triad made up of Ser-His-Asp. The activity-stability-temperature relationship is discussed in relation to those of the homologous members of the HSL group.
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