New role for leucyl aminopeptidase in glutathione turnover. (Articolo in rivista)

Type
Label
  • New role for leucyl aminopeptidase in glutathione turnover. (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1042/BJ20031336 (literal)
Alternative label
  • Cappiello M; Lazzarotti A; Buono F; Scaloni A; D'Ambrosio C; Amodeo P; Mendez BL; Pelosi P; Del Corso A; Mura U. (2004)
    New role for leucyl aminopeptidase in glutathione turnover.
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cappiello M; Lazzarotti A; Buono F; Scaloni A; D'Ambrosio C; Amodeo P; Mendez BL; Pelosi P; Del Corso A; Mura U. (literal)
Pagina inizio
  • 35 (literal)
Pagina fine
  • 44 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 378 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Fisiologia e Biochimica, Universit`a di Pisa, via S. Maria 55, 56126 Pisa, Italy, +Proteomics and Mass Spectrometry Laboratory, I.S.P.A.A.M., National Research Council, via Argine 1085, 80147 Napoli, Italy, ?Istituto di Chimica Biomolecolare, National Research Council, Via Campi Flegrei 34 - Comprensorio 'A. Olivetti' - Edificio 70, 80078 Pozzuoli (NA), Italy, and §Dipartimento di Chimica e Biotecnologie Agrarie, Universit`a di Pisa, via del Borghetto, 80, 56100 Pisa, Italy (literal)
Titolo
  • New role for leucyl aminopeptidase in glutathione turnover. (literal)
Abstract
  • A manganese-dependent cysteinyl-glycine hydrolysing activity has been purified to electrophoretic homogeneity from bovine lens. The characterization of the purified enzyme (molecular mass of the native protein, molecular mass of the subunit and extensive primary structure analysis) allowed the unequivocal attribution of the cysteinyl-glycine hydrolysing activity, which is usually associated with alanyl aminopeptidase (EC 3.4.11.2) or membrane-bound dipeptidase (EC 3.4.13.19), to LAP (leucyl aminopeptidase; EC 3.4.11.1). Analysis of the pH dependence of Cys-Gly hydrolysis catalysed by LAP, supported by a molecular modelling approach to the enzyme-substrate conformation, gave insights into the ability of the enzyme to recognize Cys-Gly as a substrate. Due to the effectiveness of LAP in hydrolysing Cys-Gly (Km = 0.57 mM, kcat = 6.0 × 103 min-1 at pH 7.4 and 25 oC) with respect to other dipeptide substrates, a new role for this enzyme in glutathione turnover is proposed. (literal)
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