Reference Report

Reference
Citation	Vallejo, C.G., Leon, P. (1989). Diadenosine 5',5''P¹,P⁴-tetraphosphatase in Drosophila embryos: developmental regulation and characterization. Int. J. Biochem. 21(11): 1223--1228. (Export to RIS)
FlyBase ID	FBrf0050097
Publication Type	Research paper
PubMed ID	2558922
PubMed Abstract	1. An enzyme has been isolated from Drosophila embryos which specifically hydrolyzes dinucleoside tetraphosphates to the corresponding nucleoside tri- and tetraphosphates, with Km values around 4 microM. 2. Nucleoside mono-, di- and triphosphates are competitive inhibitors with K1 values i the 0.01 mM range. 3. The inhibition is particularly strong by adenosine tetraphosphate (Ki = 10 nM). 4. The enzyme is maximally active at pH 7.5 and is quite stable at acid pH. 5. The enzyme requires divalent cations for activity: Co(2+) much greater than [corrected] Mn(2+) Mg(2+) x Co(2+) stimulated about 90-fold at 6 mM. 6. The specific stimulation by Co(2+) has been described before, but at lower concentrations, for the enzyme of procaryotes which splits diadenosine tetraphosphate symmetrically. Zn(2+) and Ca(2+) are inhibitors of the Drosophila enzyme. Co(2+) is also inhibitor in the presence of Mg(2+). 7. The Drosophila enzyme has essential sulphydryl group(s) and a molecular weight of 26,000. 8. Diadenosine tetraphosphatase is present in mature oocytes and increases after fertilization to reach a peak 1.5 hr later. 9. From this time to 3.5 hr the activity decreased to remain at a plateau until the end of embryogenesis. 10. The profile of activity is compatible with its involvement in the regulation of nuclear division.
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Language of Publication	English
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Publication Type	Journal
Abbreviation	Int. J. Biochem.
Title	International Journal of Biochemistry
Publication Year	1990-1994
ISBN/ISSN	0020-711X
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