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We began analyzing https://link.springer.com/article/10.1007/s00109-021-02148-1, but it redirected us to https://link.springer.com/article/10.1007/s00109-021-02148-1. The analysis below is for the second page.

Title[redir]:
Biochemical and structural characterization of beta-carbonic anhydrase from the parasite Trichomonas vaginalis | Journal of Molecular Medicine
Description:
Trichomonas vaginalis is a unicellular parasite and responsible for one of the most common sexually transmittable infections worldwide, trichomoniasis. Carbonic anhydrases (CAs) are enzymes found in all lifeforms and are known to play a vital role in many biochemical processes in organisms including the maintenance of acid–base homeostasis. To date, eight evolutionarily divergent but functionally convergent forms of CAs (α, β, γ, δ, ζ, η, θ, and ι) have been discovered. The human genome contains only α-CAs, whereas many clinically significant pathogens express only β-CAs and/or γ-CAs. The characterization of pathogenic β- and γ-CAs provides important knowledge for targeting these biomolecules to develop novel anti-invectives against trichomoniasis. Here, we report the recombinant production and characterization of the second β-CA of T. vaginalis (TvaCA2). Light scattering analysis revealed that TvaCA2 is a dimeric protein, which was further supported with in silico modeling, suggesting similar structures between TvaCA2 and the first β-CA of T. vaginalis (TvaCA1). TvaCA2 exhibited moderate catalytic activity with the following kinetic parameters: kcat of 3.8 × 105 s−1 and kcat/KM of 4.4 × 107 M−1 s−1. Enzyme activity inhibition was studied with a set of clinically used sulfonamides and sulfonamide derivates. Twenty-seven out of the 39 compounds resulted in inhibition with a nanomolar range. These initial results encourage for future work entailing the design of more potent inhibitors against TvaCA2, which may provide new assets to fight trichomoniasis. • Protozoan parasite Trichomonas vaginalis has two β-carbonic anhydrases (TvaCA1/2). • TvaCA1/TvaCA2 represents promising targets for antitrichomonal drug development. • TvaCA2 is a dimer of 20.3 kDa and possesses moderate catalytic activity. • The most efficient inhibitor was clinical drug acetazolamide with KI of 222.9 nM. • The 39 tested sulfonamides form the basis for the design of more potent inhibitors.

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Keywords {🔍}

tvaca, inhibition, article, cas, protein, google, scholar, vaginalis, anhydrase, chem, inhibitors, supuran, trichomonas, active, similar, carbonic, sequence, compound, kda, structure, med, data, compounds, site, molecular, sulfonamides, drug, size, parkkila, enzymes, profiles, determined, betacarbonic, clinically, activity, enzyme, multiple, analysis, characterization, full, hytönen, trichomoniasis, human, pathogens, drugs, chromatography, fig, image, shown, hca,

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int/mediacentre/factsheets/fs110/en/ nl/cgi-bin/emboss/supermatcher multiple sequence alignment—jabaws protozoan beta-carbonic anhydrase primary open-angle glaucoma amber99sb-ildn force field article download pdf protino® nickel-nitrilotriacetic acid poisson–boltzmann electrostatics calculations light-scattering detector based multiple sequence alignment additional c-terminal aas related subjects probable key factor stop-flow kinetic studies uk/tools/msa/clustalo full access parasite trichomonas vaginalis md-equilibrated homology model amber force field adenylyl cyclase cac1 involving multiple rounds γ-ca specific inhibitors human α-ca isozymes beta-carbonic anhydrase beta-carbonic anhydrase 1 trichomonas vaginalis increases trichomonas vaginalis homolog ni2+-nta affinity chromatography carbonic anhydrase can2 privacy choices/manage cookies trichomonas vaginalis resistant develop high-affinity inhibitors 3-bromo-4-amino-benzenesulfonamide leishmania donovani chagasi figure 1 shows require multiple rounds protozoan parasite responsible moderate/weak tvaca2 inhibition size exclusion chromatography size-exclusion chromatography standard protein samples beta-carbonic anhydrases homology modeling pathogen-specific cas clustal omega tool beta-class enzyme cryptococcus neoformans showed md-equilibrated crystal structure biomolecular drug targets

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Inhibition of Plasmodium falciparum carbonic anhydrase with aromatic sulfonamides: towards antimalarials with a novel mechanism of action?

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