Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate. (Articolo in rivista)

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Label
  • Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate. (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M104088200 (literal)
Alternative label
  • Allegrini S, Scaloni A, Ferrara L, Pesi R, Pinna P, Sgarrella F, Camici M, Eriksson S, Tozzi MG. (2001)
    Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Allegrini S, Scaloni A, Ferrara L, Pesi R, Pinna P, Sgarrella F, Camici M, Eriksson S, Tozzi MG. (literal)
Pagina inizio
  • 33526 (literal)
Pagina fine
  • 33532 (literal)
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  • http://www.jbc.org/content/276/36/33526.long (literal)
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  • 276 (literal)
Rivista
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  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Scienze del Farmaco, Università di Sassari, via Muroni 23/A, 07100 Sassari Italy and the National Laboratory of The National Institute of Biostructures and Biosystems, Osilo (Sassari), Italy, Instituto di Ricerche sull'Adattamento dei Bouini e dei Bufali nell'Ambiente del Mezzogiorno Centro Servizi di Spettrometria di Massa, via Argine 1085, 80147 Napoli, Italy, the Dipartimento di Fisiologia e Biochimica, Università di Pisa, via S. Maria, 55, 56100 Pisa, Italy, and the ?Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, The Biomedical Center, Box 575, S-751 23 Uppsala, Sweden (literal)
Titolo
  • Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate. (literal)
Abstract
  • Cytosolic 5'-nucleotidase/phosphotransferase (cN-II), specific for purine monophosphates and their deoxyderivatives, acts through the formation of a phosphoenzyme intermediate. Phosphate may either be released leading to 5'-mononucleotide hydrolysis or be transferred to an appropriate nucleoside acceptor, giving rise to a mononucleotide interconversion. Chemical reagents specifically modifying aspartate and glutamate residues inhibit the enzyme, and this inhibition is partially prevented by cN-II substrates and physiological inhibitors. Peptide mapping experiments with the phosphoenzyme previously treated with tritiated borohydride allowed isolation of a radiolabeled peptide. Sequence analysis demonstrated that radioactivity was associated with a hydroxymethyl derivative that resulted from reduction of the Asp-52-phosphate intermediate. Site-directed mutagenesis experiments confirmed the essential role of Asp-52 in the catalytic machinery of the enzyme and suggested also that Asp-54 assists in the formation of the acyl phosphate species. From sequence alignments we conclude that cytosolic 5'-nucleotidase, along with other nucleotidases, belong to a large superfamily of hydrolases with different substrate specificities and functional roles. (literal)
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