ArticleBiochemistry2009
Allosteric site variants of Haemophilus influenzae beta-carbonic anhydrase.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Bacterial β-carbonic anhydrases: a six-step prioritization framework for antibacterial target validation.Archives of microbiology · 2026Review
- Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.Science advances · 2024Article
- Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- An Overview of the Bacterial Carbonic Anhydrases.Metabolites · 2017Review
- Carbon Dioxide "Trapped" in a β-Carbonic Anhydrase.Biochemistry · 2015Article
- Bioinformatic analysis of beta carbonic anhydrase sequences from protozoans and metazoans.Parasites & vectors · 2014Article
- Nontypeable Haemophilus influenzae carbonic anhydrase is important for environmental and intracellular survival.Journal of bacteriology · 2013Article
- Biochemistry and physiology of the β class carbonic anhydrase (Cpb) from Clostridium perfringens strain 13.Journal of bacteriology · 2013Article
- Co(II)-substituted Haemophilus influenzae β-carbonic anhydrase: spectral evidence for allosteric regulation by pH and bicarbonate ion.Archives of biochemistry and biophysics · 2011Article
- Characterization of the first beta-class carbonic anhydrase from an arthropod (Drosophila melanogaster) and phylogenetic analysis of beta-class carbonic anhydrases in invertebrates.BMC biochemistry · 2010Article
- Evidence for a bicarbonate "escort" site in Haemophilus influenzae beta-carbonic anhydrase .Biochemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Haemophilus influenzae beta-carbonic anhydrase (HICA) is hypothesized to be an allosteric protein that is regulated by the binding of bicarbonate ion to a non-catalytic (inhibitory) site that controls the ligation of Asp44 to the catalytically essential zinc ion. We report here the X-ray crystallographic structures of two variants (W39F and Y181F) involved in the binding of bicarbonate ion in the non-catalytic site and an active-site variant (D44N) that is incapable of forming a strong zinc ligand. The alteration of Trp39 to Phe increases the apparent K(i) for bicarbonate inhibition by 4.8-fold. While the structures of W39F and Y181F are very similar to the wild-type enzyme, the X-ray crystal structure of the D44N variant reveals that it has adopted an active-site conformation nearly identical to that of non-allosteric beta-carbonic anhydrases. We propose that the structure of the D44N variant is likely to be representative of the active conformation of the enzyme. These results lend additional support to the hypothesis that HICA is an allosteric enzyme that can adopt active and inactive conformations, the latter of which is stabilized by bicarbonate ion binding to a non-catalytic site.
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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.