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Literature summary for 3.6.1.17 extracted from

  • Maksel, D.; Gooley, P.R.; Swarbrick, J.D.; Guranowski, A.; Gange, C.; Blackburn, G.M.; Gayler, K.R.
    Characterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifolius (2001), Biochem. J., 357, 399-405.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.17

Protein Variants

Protein Variants Comment Organism
E122Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 20% of the wild-type value, turnover-number is 50% of the wild-type value. 2.3fold reduction in sensitivity to fluoride Lupinus angustifolius
E125Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser. KM-value is 0.7% of the wild-type value, turnover-number is 56% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 83fold reduction in sensitivity to fluoride Lupinus angustifolius
E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser. KM-value is 4.8% of the wild-type value, turnover-number is 0.01% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. More than 330fold reduction in sensitivity to fluoride Lupinus angustifolius
E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 38.4% of the wild-type value, turnover-number is 9% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 16.7fold reduction in sensitivity to fluoride Lupinus angustifolius
E58Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 80% of the wild-type value, turnover-number is 43.9% of the wild-type value. 6.7fold reduction in sensitivity to fluoride Lupinus angustifolius
E59D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 4fold higher than the wild-type value, turnover-number is 0.02% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. 2fold reduction in sensitivity to fluoride Lupinus angustifolius
E59Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 2.4fold higher than the wild-type value, turnover-number is 0.00076% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected Lupinus angustifolius
R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 330fold reduction in sensitivity to fluoride Lupinus angustifolius

Inhibitors

Inhibitors Comment Organism Structure
F-
-
 Lupinus angustifolius

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
 Ap4A pH 8.0, 25°C, mutant enzyme E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser Lupinus angustifolius
0.5
-
 Ap4A pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.5
-
 Ap4A pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.96
-
 Ap4A pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
1.4
-
 Ap4A pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser Lupinus angustifolius
2
-
 Ap4A pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
2.5
-
 Ap4A pH 8.0, 25°C, wild-type enzyme Lupinus angustifolius
5.9
-
 Ap4A pH 8.0, 25°C, mutant enzyme E59Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
10
-
 Ap4A pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19120
-
 wild-type enzyme, MALDI-MS Lupinus angustifolius

Organism

Organism UniProt Comment Textmining
Lupinus angustifolius
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2'-pdA)AppppA + H2O cleavage to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP occurs with a ratio of 60:40 with the wild-type enzyme and the mutant enzymes R54Q, E58D and E125Q. With the mutants R54Q, E58D and E125Q, releasing ATP is increased to 70% of total hydrolysis. Activity of mutants E55Q, E59D and E59Q is to low to be detected Lupinus angustifolius ?
-
 ?
Ap4A + H2O
-
 Lupinus angustifolius ?
-
 ?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
 Lupinus angustifolius ATP + AMP
-
 ?

Synonyms

Synonyms Comment Organism
(asymmetrical) diadenosine 5',5''‚-P1,P4-tetraphosphate hydrolase
-
 Lupinus angustifolius
Ap4A hydrolase
-
 Lupinus angustifolius

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00031
-
 Ap4A pH 8.0, 25°C, mutant enzyme E59Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.005
-
 Ap4A pH 8.0, 25°C, mutant enzyme E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser Lupinus angustifolius
0.011
-
 Ap4A pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.29
-
 Ap4A pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser Lupinus angustifolius
3.7
-
 Ap4A pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
4.2
-
 Ap4A pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
17.9
-
 Ap4A pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
20.4
-
 Ap4A pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
40.8
-
 Ap4A pH 8.0, 25°C, wild-type enzyme Lupinus angustifolius

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.003
-
 F- pH 8.0, 25°C, wild-type enzyme Lupinus angustifolius
0.006
-
 F- pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.007
-
 F- pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.02
-
 F- pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.05
-
 F- pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius
0.25
-
 F- pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser Lupinus angustifolius
1
-
 F- pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys Lupinus angustifolius