Structural highlights
FunctionA2ENQ8_TRIV3 Reversible hydration of carbon dioxide.[RuleBase:RU003956] Publication Abstract from PubMedWe report the biochemical and structural characterisation of a beta-carbonic anhydrase (beta-CA) from Trichomonas vaginalis, a unicellular parasite responsible for one of the world's leading sexually transmitted infections, trichomoniasis. CAs are ubiquitous metalloenzymes belonging to eight evolutionarily divergent groups (alpha, beta, gamma, delta, zeta, eta, theta, and iota); humans express only alpha-CAs, whereas many clinically significant pathogens express only beta- and/or gamma-CAs. For this reason, the latter two groups of CAs are promising biomedical targets for novel antiinfective agents. The beta-CA from T. vaginalis (TvaCA1) was recombinantly produced and biochemically characterised. The crystal structure was determined, revealing the canonical dimeric fold of beta-CAs and the main features of the enzyme active site. The comparison with the active site of human CA enzymes revealed significant differences that can be exploited for the design of inhibitors selective for the protozoan enzyme with respect to the human ones. Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis.,Urbanski LJ, Di Fiore A, Azizi L, Hytonen VP, Kuuslahti M, Buonanno M, Monti SM, Angeli A, Zolfaghari Emameh R, Supuran CT, De Simone G, Parkkila S J Enzyme Inhib Med Chem. 2020 Dec;35(1):1292-1299. doi:, 10.1080/14756366.2020.1774572. PMID:32515610[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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