ArticleProceedings of the National Academy of Sciences of the United States of America2005
Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 82 citations in OpenAlex.
- Article
- Biochemical characterization of a psychrophilic and halotolerant α-carbonic anhydrase from a deep-sea bacterium,AIMS microbiology · 2023Article
- α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022Review
- Activation and thermal stabilization of a recombinant γ-glutamyltranspeptidase from Bacillus licheniformis ATCC 27811 by monovalent cations.Applied microbiology and biotechnology · 2022Article
- Crystal Structure and Active Site Engineering of a Halophilic γ-Carbonic Anhydrase.Frontiers in microbiology · 2020Article
- Bacterial γ-glutamyltranspeptidases, physiological function, structure, catalytic mechanism and application.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2020Article
- A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics.Extremophiles : life under extreme conditions · 2017Article
- Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance.BMC biotechnology · 2017Article
- Molecular Mechanisms of Enzyme Activation by Monovalent Cations.The Journal of biological chemistry · 2016Review
- Characterization of a NaCl-tolerant β-N-acetylglucosaminidase from Sphingobacterium sp. HWLB1.Extremophiles : life under extreme conditions · 2016Article
- Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst.Nature communications · 2015Article
- Salinity tolerance in plants. Quantitative approach to ion transport starting from halophytes and stepping to genetic and protein engineering for manipulating ion fluxes.Frontiers in plant science · 2015Review
- Function and biotechnology of extremophilic enzymes in low water activity.Aquatic biosystems · 2012Article
- Halophilic enzyme activation induced by salts.Scientific reports · 2011Article
- Article
- A structurally novel salt-regulated promoter of duplicated carbonic anhydrase gene 1 from Dunaliella salina.Molecular biology reports · 2010Article
- An antibiotic-resistance enzyme from a deep-sea bacterium.Journal of the American Chemical Society · 2010Article
- Structural basis for the aminoacid composition of proteins from halophilic archea.PLoS biology · 2009Article
- Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Chemical reviews · 2008Review
- Structural features that govern enzymatic activity in carbonic anhydrase from a low-temperature adapted fish, Chionodraco hamatus.Biophysical journal · 2007Article
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein molecular adaptation to drastically shifting salinities was studied in dCA II, an alpha-type carbonic anhydrase (EC 4.2.1.1) from the exceptionally salt-tolerant unicellular green alga Dunaliella salina. The salt-inducible, extracellular dCA II is highly salt-tolerant and thus differs from its mesophilic homologs. The crystal structure of dCA II, determined at 1.86-A resolution, is globally similar to other alpha-type carbonic anhydrases except for two extended alpha-helices and an added Na-binding loop. Its unusual electrostatic properties include a uniformly negative surface electrostatic potential of lower magnitude than that observed in the highly acidic halophilic proteins and an exceptionally low positive potential at a site adjoining the catalytic Zn(2+) compared with mesophilic homologs. The halotolerant dCA II also differs from typical halophilic proteins in retaining conformational stability and solubility in low to high salt concentrations. The crucial role of electrostatic features in dCA II halotolerance is strongly supported by the ability to predict the unanticipated halotolerance of the murine CA XIV isozyme, which was confirmed biochemically. A proposal for the functional significance of the halotolerance of CA XIV in the kidney is presented.
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