ArticleActa crystallographica. Section D, Biological crystallography2015
Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.Acta crystallographica. Section D, Structural biology · 2024Article
- Biochemical characterization of a psychrophilic and halotolerant α-carbonic anhydrase from a deep-sea bacterium,AIMS microbiology · 2023Article
- Inhibition of Carbonic Anhydrase Using SLC-149: Support for a Noncatalytic Function of CAIX in Breast Cancer.Journal of medicinal chemistry · 2021Article
- Aspirin: A Suicide Inhibitor of Carbonic Anhydrase II.Biomolecules · 2020Article
- The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis.Biochemistry · 2016Article
- Activity and anion inhibition studies of the α-carbonic anhydrase from Thiomicrospira crunogena XCL-2 Gammaproteobacterium.Bioorganic & medicinal chemistry letters · 2015Article
- Observed surface lysine acetylation of human carbonic anhydrase II expressed in Escherichia coli.Protein science : a publication of the Protein Society · 2015Article
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10 authors.
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Abstract
Biocatalytic CO2 sequestration to reduce greenhouse-gas emissions from industrial processes is an active area of research. Carbonic anhydrases (CAs) are attractive enzymes for this process. However, the most active CAs display limited thermal and pH stability, making them less than ideal. As a result, there is an ongoing effort to engineer and/or find a thermostable CA to fulfill these needs. Here, the kinetic and thermal characterization is presented of an α-CA recently discovered in the mesophilic hydrothermal vent-isolate extremophile Thiomicrospira crunogena XCL-2 (TcruCA), which has a significantly higher thermostability compared with human CA II (melting temperature of 71.9°C versus 59.5°C, respectively) but with a tenfold decrease in the catalytic efficiency. The X-ray crystallographic structure of the dimeric TcruCA shows that it has a highly conserved yet compact structure compared with other α-CAs. In addition, TcruCA contains an intramolecular disulfide bond that stabilizes the enzyme. These features are thought to contribute significantly to the thermostability and pH stability of the enzyme and may be exploited to engineer α-CAs for applications in industrial CO2 sequestration.
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