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J Enzyme Inhib Med Chem. 2016;31(sup4):176-184. Epub 2016 Aug 25.

Identification and inhibition of carbonic anhydrases from nematodes.

Author information

1
a School of Medicine, University of Tampere , Tampere , Finland.
2
b BioMediTech, University of Tampere , Tampere , Finland.
3
c Fimlab Laboratories Ltd and Tampere University Hospital , Tampere , Finland.
4
d Department of Otorhinolaryngology , Central Finland Central Hospital , Jyväskylä , Finland , and.
5
e Neurofarba Dipartment, Sezione di Scienza Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze , Firenze , Italy.

Abstract

Carbonic anhydrases (CAs) are metalloenzymes, and classified into the evolutionarily distinct α, β, γ, δ, ζ, and η classes. α-CAs are present in many living organisms. β- and γ-CAs are expressed in most prokaryotes and eukaryotes, except for vertebrates. δ- and ζ-CAs are present in phytoplanktons, and η-CAs have been found in Plasmodium spp. Since the identification of α- and β-CAs in Caenorhabditis elegans, the nematode CAs have been considered as an emerging target in research focused on antiparasitic CA inhibitors. Despite the presence of α-CAs in both helminths and vertebrates, structural studies have revealed different kinetic and inhibition results. Moreover, lack of β-CAs in vertebrates makes this enzyme as an attractive target for inhibitory studies against helminthic infection. Some CA inhibitors, such as sulfonamides, have been evaluated against nematode CAs. This review article aims to present comprehensive information about the nematode CAs and their inhibitors as potential anthelminthic drugs.

KEYWORDS:

Acetazolamide; carbonic anhydrase; carbonic anhydrase inhibitors; nematode; sulfonamide

PMID:
27557594
DOI:
10.1080/14756366.2016.1221826
[Indexed for MEDLINE]

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