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Título

Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates

AutorGuranowski, Andrzej; Sillero, Antonio ; Günther Sillero, María A.
Palabras clave3'-Adenylated dinucleoside polyphosphates
Diadenosine triphosphate
Diadenosine tetraphosphate
Diguanosine tetraphosphate
Diadenosine triphosphatase
Diadenosine tetraphosphatase
Fecha de publicación2003
EditorPolish Academy of Sciences
CitaciónActa Biochimica Polonica 50(1): 123-130 (2003)
ResumenSeveral 3'-[32P]adenylated dinucleoside polyphosphates (NpnN'p*As) were synthesized by the use of poly(A) polymerase (Sillero MAG et al., 2001, Eur J Biochem.; 268 : 3605-11) and three of them, ApppA[32P]A or ApppAp*A, AppppAp*A and GppppGp*A, were tested as potential substrates of different dinucleoside polyphosphate degrading enzymes. Human (asymmetrical) dinucleoside tetraphosphatase (EC 3.6.1.17) acted almost randomly on both AppppAp*A, yielding approximately equal amounts of pppA + pAp*A and pA + pppAp*A, and GppppGp*, yielding pppG + pGp*A and pG + pppGp*A. Narrow-leafed lupin (Lupinus angustifolius) tetraphosphatase acted preferentially on the dinucleotide unmodified end of both AppppAp*A (yielding 90% of pppA + pAp*A and 10 % of pA + pppAp*A) and GppppGp*A (yielding 89% pppG + pGp*A and 11% of pG + pppGp*A). (Symmetrical) dinucleoside tetraphosphatase (EC 3.6.1.41) from Escherichia coli hydrolyzed AppppAp*A and GppppGp*A producing equal amounts of ppA + ppAp*A and ppG + ppGp*A, respectively, and, to a lesser extent, ApppAp*A producing pA + ppAp*A. Two dinucleoside triphosphatases (EC 3.6.1.29) (the human Fhit protein and the enzyme from yellow lupin (Lupinus luteus)) and dinucleoside tetraphosphate phosphorylase (EC 2.7.7.53) from Saccharomyces cerevisiae did not degrade the three 3'-adenylated dinucleoside polyphosphates tested.
Descripción8 pages, 3 figures, 1 table.
Versión del editorhttp://yadda.icm.edu.pl/przyrbwn/details/journal/article.nav?id=bwmeta1.element.bwnjournal-article-abpv50i1p123kz&stitle=Selective%20splitting%20of%203%27-adenylated%20dinucleoside%20polyphosphates%20by%20specific%20enzymes%20degrading%20dinucleoside%20polyphosphates&sjournal=Acta%20Biochimica%20Polonica&cid=se997
URIhttp://hdl.handle.net/10261/24479
ISSN0001-527X
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