ArticleScientific reports2016
Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Exploring archaeal resources for biomass-derived pentose utilization: pathways, extremozymes, and bioprocessing applications.World journal of microbiology & biotechnology · 2026Review
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Gene Detection and Enzymatic Activity of PsychrotrophicMicroorganisms · 2025Article
- Cloning, Expression, Characterization and Immobilization of a Recombinant Carboxylesterase from the Halophilic Archaeon,Biomolecules · 2024Article
- Biochemical characterization of an esterase from Clostridium acetobutylicum with novel GYSMG pentapeptide motif at the catalytic domain.Journal of industrial microbiology & biotechnology · 2020Article
- Engineering a Seven Enzyme Biotransformation using Mathematical Modelling and Characterized Enzyme Parts.ChemCatChem · 2019Article
- Improving the 'tool box' for robust industrial enzymes.Journal of industrial microbiology & biotechnology · 2017Review
- Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases.Scientific reports · 2016Article
- Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator.The Journal of biological chemistry · 2016Article
- EstDZ3: A New Esterolytic Enzyme Exhibiting Remarkable Thermostability.Frontiers in microbiology · 2016Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
A new carboxyl esterase, AF-Est2, from the hyperthermophilic archaeon Archaeoglobus fulgidus has been cloned, over-expressed in Escherichia coli and biochemically and structurally characterized. The enzyme has high activity towards short- to medium-chain p-nitrophenyl carboxylic esters with optimal activity towards the valerate ester. The AF-Est2 has good solvent and pH stability and is very thermostable, showing no loss of activity after incubation for 30 min at 80 °C. The 1.4 Å resolution crystal structure of AF-Est2 reveals Coenzyme A (CoA) bound in the vicinity of the active site. Despite the presence of CoA bound to the AF-Est2 this enzyme has no CoA thioesterase activity. The pantetheine group of CoA partially obstructs the active site alcohol pocket suggesting that this ligand has a role in regulation of the enzyme activity. A comparison with closely related α/β hydrolase fold enzyme structures shows that the AF-Est2 has unique structural features that allow CoA binding. A comparison of the structure of AF-Est2 with the human carboxyl esterase 1, which has CoA thioesterase activity, reveals that CoA is bound to different parts of the core domain in these two enzymes and approaches the active site from opposite directions.
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