ArticleProtein science : a publication of the Protein Society2018
Structural insights into a thermostable variant of human carbonic anhydrase II.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Time-Resolved Native Mass Spectrometry for Direct Measurement of Biomolecular Kinetics.Journal of the American Chemical Society · 2026Article
- Comparative Analysis of Carbonic Anhydrase-II Expression Across Undescended Testes Sprague Dawley Model with Coenzyme Q10 Treatment.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2025Article
- Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions.Nature communications · 2024Article
- Evaluation of Human Carbonic Anhydrase II (CA-II) Concentration Using ELISA: Insights into Optical Density's Role in Biomarker Quantification for Cryptorchidism Research.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2024Article
- Structural and thermodynamic analysis of factors governing the stability and thermal folding/unfolding of SazCA.PloS one · 2021Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbonic anhydrase is an enzyme of interest for many biotechnological developments including carbon sequestration. These applications often require harsh conditions, so there is a need for the development of thermostable variants. One of the most thermostable human carbonic anhydrase II (HCAIIts) variants was patented in 2006. Here, we report the ultra-high resolution crystal structure of HCAIIts. The structural changes seen are consistent with each of the six mutations involved acting largely independently and variously resulting in increased H-bonding, improved packing, and reduced side chain entropy loss on folding to yield the increased stability. We further suggest that for four of the mutations, improvements in backbone conformational energetics is also a contributor and that considerations of such conformational propensities of individual amino acids are often overlooked.
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