ArticleBiochemistry2015
Carbon Dioxide "Trapped" in a β-Carbonic Anhydrase.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- Structural characterization and inhibition of carbonic anhydrase fromJournal of structural biology: X · 2025Article
- Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Streamlining heterologous expression of top carbonic anhydrases in Escherichia coli: bioinformatic and experimental approaches.Microbial cell factories · 2024Article
- Expression and localization of two β-carbonic anhydrases inFrontiers in plant science · 2024Article
- Carbonic anhydrase versatility: from pH regulation to COFrontiers in molecular biosciences · 2023Article
- Anion inhibition studies of the α-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2021Article
- An anion and small molecule inhibition study of the β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.Journal of enzyme inhibition and medicinal chemistry · 2021Review
- Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis.Nature structural & molecular biology · 2021Article
- Zeta-carbonic anhydrases show CSComputational and structural biotechnology journal · 2021Article
- Mobility of Lewis acids within the secondary coordination sphere: toward a model for cooperative substrate binding.Chemical communications (Cambridge, England) · 2020Article
- Pyropia yezoensis genome reveals diverse mechanisms of carbon acquisition in the intertidal environment.Nature communications · 2020Article
- Kinetic study of catalytic CORoyal Society open science · 2019Article
- Carbonic Anhydrases: Nature's Way to Balance COBiochemistry & molecular biology journal · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a β-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 Å resolution with R(cryst) and R(free) values of 17.3 and 19.9%, respectively, and is compared with the α-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.