ArticlePloS one2017
Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 36 citations in OpenAlex.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Experimental, Genomic, and Structural Evidence Supporting Putative PET-Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru.MicrobiologyOpen · 2026Article
- Optimization, purification and characterization of an intracellular salt-tolerant esterase Est40 from Vreelandella sp. CH40.Archives of microbiology · 2025Article
- Abridgement of Microbial Esterases and Their Eminent Industrial Endeavors.Molecular biotechnology · 2025Review
- Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic BacteriumInternational journal of molecular sciences · 2023Article
- Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.PloS one · 2023Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation.International journal of molecular sciences · 2022Review
- Characterization and purification of esterase from Cellulomonas fimi DB19 isolated from Zanthoxylum armatum with its possible role in diesel biodegradation.Archives of microbiology · 2022Article
- Xerotolerance: A New Property inMicroorganisms · 2021Article
- Article
- Biochemical characterization of an esterase from Clostridium acetobutylicum with novel GYSMG pentapeptide motif at the catalytic domain.Journal of industrial microbiology & biotechnology · 2020Article
- Characterization and Immobilization of a Novel SGNH Family Esterase (International journal of molecular sciences · 2019Article
- Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity (Biomolecules · 2019Article
- Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (Biomolecules · 2019Article
- Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action.Molecules (Basel, Switzerland) · 2019Review
- Crystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor.Scientific reports · 2018Article
- Article
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12 authors at 4 institutions in 1 country.
Funding
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Abstract
A novel microbial esterase, EaEST, from a psychrophilic bacterium Exiguobacterium antarcticum B7, was identified and characterized. To our knowledge, this is the first report describing structural analysis and biochemical characterization of an esterase isolated from the genus Exiguobacterium. Crystal structure of EaEST, determined at a resolution of 1.9 Å, showed that the enzyme has a canonical α/β hydrolase fold with an α-helical cap domain and a catalytic triad consisting of Ser96, Asp220, and His248. Interestingly, the active site of the structure of EaEST is occupied by a peracetate molecule, which is the product of perhydrolysis of acetate. This result suggests that EaEST may have perhydrolase activity. The activity assay showed that EaEST has significant perhydrolase and esterase activity with respect to short-chain p-nitrophenyl esters (≤C8), naphthyl derivatives, phenyl acetate, and glyceryl tributyrate. However, the S96A single mutant had low esterase and perhydrolase activity. Moreover, the L27A mutant showed low levels of protein expression and solubility as well as preference for different substrates. On conducting an enantioselectivity analysis using R- and S-methyl-3-hydroxy-2-methylpropionate, a preference for R-enantiomers was observed. Surprisingly, immobilized EaEST was found to not only retain 200% of its initial activity after incubation for 1 h at 80°C, but also retained more than 60% of its initial activity after 20 cycles of reutilization. This research will serve as basis for future engineering of this esterase for biotechnological and industrial applications.
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