http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51477
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)
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- 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)
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- http://www.jbc.org/content/276/36/33526.long (literal)
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- 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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