Recent Advances in Research on the Most Novel Carbonic Anhydrases, CA XIII and XV (Articolo in rivista)

Type
Label
  • Recent Advances in Research on the Most Novel Carbonic Anhydrases, CA XIII and XV (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.2174/138161208783877811 (literal)
Alternative label
  • Hilvo M; Innocenti A; Monti SM; De Simone G; Supuran CT; Parkkila S. (2008)
    Recent Advances in Research on the Most Novel Carbonic Anhydrases, CA XIII and XV
    in Current pharmaceutical design (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Hilvo M; Innocenti A; Monti SM; De Simone G; Supuran CT; Parkkila S. (literal)
Pagina inizio
  • 672 (literal)
Pagina fine
  • 678 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 14 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Review (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Medical Technology and School of Medicine, University of Tampere and Tampere University Hospital, Biokatu 6, 33014 University of Tampere, Finland; Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Room 188, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy; Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Naples, Italy. (literal)
Titolo
  • Recent Advances in Research on the Most Novel Carbonic Anhydrases, CA XIII and XV (literal)
Abstract
  • The carbonic anhydrase (CA) enzyme family consists of thirteen active isozymes in mammals. The most recently characterized members of this family are cytosolic CA XIII and membrane-bound CA XV. This article describes recent advances in the CA family, especially CA XIII and XV. We have also included catalytic activity data on human CA XIII and mouse CA XV. Additionally, the inhibition constants of acetazolamide toward these isozymes were determined to be kcat = 1.5 x 105 s-1, kcat/KM = 1.1 x 107 M-1s-1 and KI = 16 nM for human CA XIII and kcat= 4.7 x 105 s-1, kcat/KM = 3.3 x 107 M-1s-1 and KI = 72 nM for mouse CA XV. Although the activity of CA XIII is the second lowest reported thus far for any of the human CAs, it may have a role in maintaining the acid-base balance in the kidney and the gastrointestinal and reproductive tracts. CA XV is an exceptional enzyme, as it seems to be active in numerous species, such as rodents, birds and fish, but is absent from humans and chimpanzees. Mouse CA XV is a moderately active enzyme, suggesting that it may play a physiological role at least in the kidney. It is likely that other isozymes have substituted for this protein in humans. In addition to the novel data on CA XIII and XV, we present the catalytic activities as well as inhibition constants of acetazolamide for all mammalian CA isozymes in this review. (literal)
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