The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines. (Articolo in rivista)

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  • The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines. (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bmcl.2012.08.088 (literal)
Alternative label
  • Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b, (2012)
    The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines.
    in Bioorganic and medicinal chemistry letters (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Daniela Vullo a, Viviana De Luca b, Andrea Scozzafava a, Vincenzo Carginale b, Mosè Rossi b, c, Claudiu T. Supuran a, d, Clemente Capasso b, (literal)
Pagina inizio
  • 6324 (literal)
Pagina fine
  • 6327 (literal)
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  • http://www.sciencedirect.com/science/article/pii/S0960894X12010992 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 22 (literal)
Rivista
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  • 4 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 20 (literal)
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  • a Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy b Istituto di Biochimica delle Proteine - CNR, Via P. Castellino 111, 80131 Napoli, Italy c Centro di Ricerca Interdipartimentale sui Biomateriali, Univ. Federico II, P-le V. Tecchio 80, 80125 Napoli, Italy d Università degli Studi di Firenze, Polo Scientifico, Dipartimento di Scienze Farmaceutiche, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy (literal)
Titolo
  • The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines. (literal)
Abstract
  • The ?-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its activation with a series of amino acids and amines. D-His, L-Phe, L-Tyr, L- and D-Trp were the most effective SspCA activators, with activation constants in the range of 1-12 nM, whereas L-His, L/D-DOPA, D-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (K(A) in the range of 37 nM-0.97 ?M). The least effective SspCA activator was d-Phe (K(A) of 5.13 ?M). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO(2) capture processes. (literal)
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