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

• Autorzy: Guranowski A. , Sillero A. , Gunther-Sillero M.A.
• Języki publikacji: EN

Abstrakty

EN

Several 3' -[32 P]adenylated dinucleoside polyphosphates (NpnN' p*As) were synthe­sized by the use of poly(A) polymerase (Sillero MAG etal., 2001, Eur JBiochem.; 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.

Słowa kluczowe

EN

diguanosine tetraphosphate; diadenosine tetraphosphate; polyphosphate; diadenosine tetraphosphatase; enzyme; diadenosine triphosphate; 3'-adenylated dinucleoside polyphosphate; diadenosine triphosphatase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 1
• Opis fizyczny: p.123-130,fig.

Twórcy

autor

Guranowski A.

• Agricultural University, Wolynska 35, 60-637 Poznan, Poland

autor

Sillero A.

autor

Gunther-Sillero M.A.

Bibliografia

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