ArticleJournal of enzyme inhibition and medicinal chemistry2017
A one-step procedure for immobilising the thermostable carbonic anhydrase (SspCA) on the surface membrane of Escherichia coli.
Article in Journal of enzyme inhibition and medicinal chemistry, 2017. 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, 24 citations in OpenAlex.
- Immobilization of carbonic anhydrase for COApplied microbiology and biotechnology · 2022Review
- Surface display of carbonic anhydrase onSynthetic and systems biotechnology · 2022Article
- Evaluating the efficiency of enzyme accelerated COJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Decorating the surface of Escherichia coli with bacterial lipoproteins: a comparative analysis of different display systems.Microbial cell factories · 2021Article
- Use of an immobilised thermostableJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Review
- Thermostability enhancement of the α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense by using the anchoring-and-self-labelling-protein-tag system (ASLJournal of enzyme inhibition and medicinal chemistry · 2019Article
- An AGT-based protein-tag system for the labelling and surface immobilization of enzymes on E. coli outer membrane.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Inhibition of Shiga toxin-converting bacteriophage development by novel antioxidant compounds.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- An Overview of the Bacterial Carbonic Anhydrases.Metabolites · 2017Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The carbonic anhydrase superfamily (CA, EC 4.2.1.1) of metalloenzymes is present in all three domains of life (Eubacteria, Archaea, and Eukarya), being an interesting example of convergent/divergent evolution, with its seven families (α-, β-, γ-, δ-, ζ-, η-, and θ-CAs) described so far. CAs catalyse the simple, but physiologically crucial reaction of carbon dioxide hydration to bicarbonate and protons. Recently, our groups characterised the α-CA from the thermophilic bacterium, Sulfurihydrogenibium yellowstonense finding a very high catalytic activity for the CO
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Registered trials
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