Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis

Autor: Latifeh Azizi, Vesa P. Hytönen, Simona Maria Monti, Claudiu T. Supuran, Giuseppina De Simone, Reza Zolfaghari Emameh, Martina Buonanno, Linda J Urbański, Marianne Kuuslahti, Andrea Angeli, Seppo Parkkila, Anna Di Fiore
Rok vydání: 2020
Předmět:
Zdroj: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 35, Iss 1, Pp 1292-1299 (2020)
Journal of Enzyme Inhibition and Medicinal Chemistry
article-version (VoR) Version of Record
ISSN: 1475-6374
1475-6366
Popis: We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-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 (α, β, γ, δ, ζ, η, θ, and ι); humans express only α-CAs, whereas many clinically significant pathogens express only β- and/or γ-CAs. For this reason, the latter two groups of CAs are promising biomedical targets for novel antiinfective agents. The β-CA from T. vaginalis (TvaCA1) was recombinantly produced and biochemically characterised. The crystal structure was determined, revealing the canonical dimeric fold of β-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.
Databáze: OpenAIRE
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