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Literature summary extracted from

  • Winward, L.; Whitfield, W.G.; Woodman, T.J.; McLennan, A.G.; Safrany, S.T.
    Characterisation of a bis(5-nucleosyl)-tetraphosphatase (asymmetrical) from Drosophila melanogaster (2007), Int. J. Biochem. Cell Biol., 39, 943-954.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.17 DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged Apf in Spodoptera frugiperda Sf21 cells, expression of EGFP-tagged enzyme in Drosophila melanbogaster Mel-2 cells Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.17 fluoride fluoride potently inhibits diadenosine tetraphosphate hydrolysis in the presence of Mg2+, whereas it is ineffective in the presence of Zn2+, because inhibition involves a specific, MgF3--containing transition state analogue complex, overview Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.17 additional information
-
additional information kinetics strongly depend on pH and cation, overview Drosophila melanogaster
3.6.1.17 0.009
-
5',5'-diadenosine tetraphosphate pH 6.5, 1 mm Zn2+ Drosophila melanogaster
3.6.1.17 0.012
-
5',5'-diadenosine tetraphosphate pH 7.5, 20 mM Mg2+ Drosophila melanogaster
3.6.1.17 0.015
-
5',5'-diadenosine hexaphosphate pH 7.5, 20 mM Mg2+ Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.17 nucleus association with euchromatin and facultative heterochromatin Drosophila melanogaster 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.17 Co2+ the enzyme is dependent on divalent cations Drosophila melanogaster
3.6.1.17 Mg2+ the enzyme is dependent on divalent cations, preferred cation, best at 3-10 mM Drosophila melanogaster
3.6.1.17 Mn2+ the enzyme is dependent on divalent cations Drosophila melanogaster
3.6.1.17 additional information no activation by Cu2+, Fe2+, Ni2+ or Ca2+ Drosophila melanogaster
3.6.1.17 Zn2+ the enzyme is dependent on divalent cations, high activity Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.17 5',5'-diadenosine tetraphosphate + H2O Drosophila melanogaster
-
ATP + AMP
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.17 Drosophila melanogaster Q4V6M1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.17 recombinant His-tagged Apf from Spodoptera frugiperda Sf21 cells by nickel affinity chromatography with removal of the His-tag Drosophila melanogaster

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.17 additional information patterns of Apf expression in Drosophila melanogaster tissues, semi-quantitative RT-PCR, highest expression levels in embryos and adult females, overview Drosophila melanogaster
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.17 additional information
-
-
Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.17 5',5'-diadenosine hexaphosphate + H2O diadenosine hexaphosphate is efficiently hydrolysed to ATP only at pH 7.5 with 20 mM Mg2+ Drosophila melanogaster 2 ATP
-
?
3.6.1.17 5',5'-diadenosine pentaphosphate + H2O
-
Drosophila melanogaster ATP + ADP
-
?
3.6.1.17 5',5'-diadenosine tetraphosphate + H2O
-
Drosophila melanogaster ATP + AMP
-
?
3.6.1.17 5',5'-diadenosine tetraphosphate + H2O best substrate Drosophila melanogaster ATP + AMP
-
?
3.6.1.17 adenosine-5'-pentaphospho-5'-guanosine + H2O
-
Drosophila melanogaster ?
-
?
3.6.1.17 adenosine-5'-tetraphospho-5'-guanosine + H2O
-
Drosophila melanogaster ?
-
?
3.6.1.17 additional information Apf always produces an NTP product, with substrate preference depending on pH and divalent ion Drosophila melanogaster ?
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.17 More the enzyme contains a Nudix motif Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
3.6.1.17 Ap4A hydrolase
-
Drosophila melanogaster
3.6.1.17 Apf
-
Drosophila melanogaster
3.6.1.17 More Apf is a typical member of the bis (5'-nucleosyl)-tetraphosphatase subfamily of Nudix hydrolases Drosophila melanogaster
3.6.1.17 Nudix hydrolase
-
Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.17 25 40 broad optimum Drosophila melanogaster

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.1.17 20 60 65% of maximal activity at 52°C Drosophila melanogaster

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.17 60
-
20 min, 55% remaining activity Drosophila melanogaster
3.6.1.17 95
-
20 min, 1 mM Mn2+, a little amount of activity is remaining Drosophila melanogaster

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.17 4
-
5',5'-diadenosine hexaphosphate pH 7.5, 20 mM Mg2+ Drosophila melanogaster
3.6.1.17 13
-
5',5'-diadenosine tetraphosphate pH 7.5, 20 mM Mg2+ Drosophila melanogaster
3.6.1.17 43
-
5',5'-diadenosine tetraphosphate pH 6.5, 1 mM Zn2+ Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.17 6.5 7.5 activity depends on the substrate and the divalent cation Drosophila melanogaster

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.6.1.17 0.02
-
in presence of Mg2+ Drosophila melanogaster fluoride