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(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
(phosphate)13-18 + H2O
(phosphate)12-17 + phosphate
(phosphate)15 + H2O
(phosphate)14 + phosphate
(phosphate)208 + H2O
(phosphate)207 + phosphate
(phosphate)25 + H2O
(phosphate)24 + phosphate
(phosphate)3 + H2O
(phosphate)2 + phosphate
(phosphate)300 + H2O
(phosphate)299 + phosphate
(phosphate)4 + H2O
(phosphate)3 + phosphate
-
-
-
-
?
(phosphate)45 + H2O
(phosphate)44 + phosphate
(phosphate)65 + H2O
(phosphate)64 + phosphate
(phosphate)9 + H2O
(phosphate)8 + phosphate
45% of the activity with (phosphate)25
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
(polyphosphate)130 + H2O
(polyphosphate)129 + phosphate
(polyphosphate)14 + H2O
(polyphosphate)13 + phosphate
(polyphosphate)60 + H2O
(polyphosphate)59 + phosphate
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
adenosine 5'-pentaphosphate + H2O
?
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
ADP + H2O
AMP + phosphate
ATP + 2 H2O
AMP + 2 phosphate
cAMP + H2O
adenosine + phosphate
diphosphate + H2O
2 phosphate
GTP + H2O
GDP + phosphate
guanosine 5'-tetraphosphate + H2O
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
inosine tetraphosphate + H2O
ITP + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
polyP10 + H2O
polyP9 + phosphate
polyP100 + H2O
polyP99 + phosphate
-
-
-
-
?
polyP15 + H2O
polyP14 + phosphate
-
-
-
-
?
polyP208 + H2O
polyP207 + phosphate
-
-
-
-
?
polyP25 + H2O
polyP24 + phosphate
-
-
-
-
?
polyP250 + H2O
polyP249 + phosphate
-
-
-
-
?
polyP33-36
polyP32-35 + phosphate
-
-
-
-
?
polyP50 + H2O
polyP49 + phosphate
-
-
-
-
?
polyP500
polyP499 + phosphate
-
-
-
-
?
polyP500 + H2O
polyP499 + phosphate
-
-
-
-
?
polyP9-10
polyP8-9 + phosphate
-
-
-
-
?
polyphosphate + H2O
?
-
chain length of more than 45 phosphate residues
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
polyphosphate 188 + H2O
polyphosphate 187 + phosphate
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
polyphosphate 75 + H2O
polyphosphate 74 + phosphate
-
-
-
-
?
polyphosphate glass type 15 + H2O
?
-
-
-
-
?
polyphosphate130 + H2O
polyphosphate129 + phosphate
polyphosphate208 + H2O
?
-
-
-
?
polyphosphate25 + H2O
polyphosphate24 + phosphate
polyphosphate3 + H2O
diphosphate + phosphate
polyphosphate45 + H2O
polyphosphate44 + phosphate
-
-
-
-
?
polyphosphate60 + H2O
polyphosphate59 + phosphate
polyphosphate65 + H2O
polyphosphate64 + phosphate
polyphosphate700 + H2O
polyphosphate699 + phosphate
polyphosphate75 + H2O
polyphosphate74 + phosphate
-
-
-
-
?
sodium phosphate glass type 15 + H2O
? + phosphate
-
-
-
-
?
tetraphosphate + H2O
triphosphate + phosphate
-
-
-
?
triphosphate + H2O
?
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
tripolyphosphate + H2O
phosphate + ?
additional information
?
-
(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
-
-
-
?
(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
-
-
-
-
?
(phosphate)13-18 + H2O
(phosphate)12-17 + phosphate
-
-
-
?
(phosphate)13-18 + H2O
(phosphate)12-17 + phosphate
-
-
-
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
-
-
-
-
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
-
-
-
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
88% of the activity with (phosphate)25
-
-
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
-
reaction continues to a chain length of about 15 residues
-
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
100% activity
-
-
?
(phosphate)25 + H2O
(phosphate)24 + phosphate
-
-
-
-
?
(phosphate)25 + H2O
(phosphate)24 + phosphate
100% activity
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
-
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
best substrate
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
-
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
best substrate
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
-
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
14% of the activity with (phosphate)25
-
-
?
(phosphate)300 + H2O
(phosphate)299 + phosphate
or even longer chain length
-
-
?
(phosphate)300 + H2O
(phosphate)299 + phosphate
or even longer chain length
-
-
?
(phosphate)45 + H2O
(phosphate)44 + phosphate
-
-
-
-
?
(phosphate)45 + H2O
(phosphate)44 + phosphate
100% activity
-
-
?
(phosphate)65 + H2O
(phosphate)64 + phosphate
-
-
-
-
?
(phosphate)65 + H2O
(phosphate)64 + phosphate
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
degradation of polyphosphate
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
h-prune efficiently hydrolyzes short-chain polyphosphates
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
regulatory enzyme in polyphosphate metabolism
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
the cytosolic exopolyphosphatase that processively cleaves the terminal phosphate group from the polyphosphate chain, until inorganic diphosphate is all that remains, structure of the substrate binding channel, overview
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)130 + H2O
(polyphosphate)129 + phosphate
-
-
-
?
(polyphosphate)130 + H2O
(polyphosphate)129 + phosphate
-
-
-
?
(polyphosphate)14 + H2O
(polyphosphate)13 + phosphate
-
-
-
?
(polyphosphate)14 + H2O
(polyphosphate)13 + phosphate
-
-
-
?
(polyphosphate)60 + H2O
(polyphosphate)59 + phosphate
-
-
-
?
(polyphosphate)60 + H2O
(polyphosphate)59 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
phosphate starvation induces the formation of the enzyme
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
enzyme is derepressed under phosphate starvation conditions
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
n = 500
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
no acyivity if n = 200
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
n = 40, 72, 180 or 290, highest reaction rate, when n is 40
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
polyphosphatase I shows optimal activity when n is 25 phosphate residues, polyphosphatases II prefers substrates with 9 residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
ir
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
n = 500 - 600
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
the activity with polyP15 is 85% of that with polyP208, the activity with polyP9 is 24% of that with polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
poly P9-10, polyP33-36
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
n = 10, 25, 50, 100, 250 or 500. n = 250 is the preferred substrate
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
polyP15, polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
chain length of 10-200 phosphate residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
chain length of 10-200 phosphate residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
the inhibitory effect of long-chain polyphosphates on adenylate kinase is higher than that of short-chain polyphosphates, suggesting a potential role of polyphosphate metabolism in regulating intracellular concentration of adenylate nucleotides
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
7.3% of the activity with polyP208
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
cAMP + H2O
adenosine + phosphate
-
-
-
?
cAMP + H2O
adenosine + phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
-
?
diphosphate + H2O
2 phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
guanosine 5'-tetraphosphate + H2O
?
-
-
-
-
?
guanosine 5'-tetraphosphate + H2O
?
-
-
-
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
-
-
-
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
-
-
-
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
-
-
-
-
?
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
-
-
-
?
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
-
-
-
?
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
-
-
-
-
?
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
-
-
-
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
-
-
-
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
-
-
-
?
polyP10 + H2O
polyP9 + phosphate
-
-
-
-
?
polyP10 + H2O
polyP9 + phosphate
-
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
-
-
-
?
polyphosphate130 + H2O
polyphosphate129 + phosphate
-
-
-
?
polyphosphate130 + H2O
polyphosphate129 + phosphate
-
-
-
?
polyphosphate25 + H2O
polyphosphate24 + phosphate
-
-
-
?
polyphosphate25 + H2O
polyphosphate24 + phosphate
-
-
-
-
?
polyphosphate3 + H2O
diphosphate + phosphate
-
-
-
-
?
polyphosphate3 + H2O
diphosphate + phosphate
-
-
-
?
polyphosphate60 + H2O
polyphosphate59 + phosphate
-
-
-
?
polyphosphate60 + H2O
polyphosphate59 + phosphate
-
-
-
?
polyphosphate65 + H2O
polyphosphate64 + phosphate
-
-
-
?
polyphosphate65 + H2O
polyphosphate64 + phosphate
-
-
-
-
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
-
-
-
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
-
-
-
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
tripolyphosphate + H2O
phosphate + ?
-
-
-
-
?
tripolyphosphate + H2O
phosphate + ?
-
7.3% of the activity with polyP208
-
-
?
additional information
?
-
isoform Ppx1 shows substantial nucleoside triphosphatase activity
-
-
?
additional information
?
-
isoform Ppx1 shows substantial nucleoside triphosphatase activity
-
-
?
additional information
?
-
isoform Ppx1 shows substantial nucleoside triphosphatase activity
-
-
?
additional information
?
-
isoform Ppx1 shows substantial nucleoside triphosphatase activity
-
-
?
additional information
?
-
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
-
-
?
additional information
?
-
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
-
-
?
additional information
?
-
-
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
-
-
?
additional information
?
-
-
contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
-
-
?
additional information
?
-
exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
-
-
-
additional information
?
-
-
exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
-
-
-
additional information
?
-
substrates are commercial sodium phosphate glass with 25-PP25-, 65-PP65-, or PPK-synthesized polyphosphate with 700-PP700-average number of residues. Released phosphate is detected by the malachite green method at 630 nm
-
-
-
additional information
?
-
-
substrates are commercial sodium phosphate glass with 25-PP25-, 65-PP65-, or PPK-synthesized polyphosphate with 700-PP700-average number of residues. Released phosphate is detected by the malachite green method at 630 nm
-
-
-
additional information
?
-
-
contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
-
-
?
additional information
?
-
-
h-prune is the missing exopolyphosphatase in animals and support the hypothesis that the metastatic effects of h-prune are modulated by inorganic polyphosphates, which are increasingly recognized as critical regulators in cells
-
-
?
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
?
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
-
-
-
additional information
?
-
the enzyme does not cleave ppGpp
-
-
?
additional information
?
-
-
the enzyme does not cleave ppGpp
-
-
?
additional information
?
-
no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
-
-
?
additional information
?
-
-
no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
-
-
?
additional information
?
-
the enzyme does not cleave ppGpp
-
-
?
additional information
?
-
no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
-
-
?
additional information
?
-
-
Pseudomonas aeruginosa exopolyphosphatase catalyzes the hydrolysis of polyphosphates (polyP), producing polyphosphate_n-1 plus inorganic phosphate, but the exopolyphosphatase is also a polyphosphate:ADP phosphotransferase. 0.1 ml of enzyme and polyphosphate substrate in 50 mM Tris-HCl, pH 8.0, 80 mM KCl, and 5 mM MgCl2 are mixed with 0.4 ml of a solution with 2.5% (NH4)6Mo7O24 x (H2O)4 in 3 NH2SO4 and 0.4 ml of 2% ascorbic acid/2% hydrazine in 0.1 NH2SO4, and the solution is brought to a final volume of 1.2 ml with triple glass-distilled water. Quantification of free phosphate is performed after 30 min of incubation at 37°C through measurement of the absorbance at 820 nm
-
-
-
additional information
?
-
-
the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
-
-
-
additional information
?
-
-
the recombinant enzyme rRmPPase, a inorganic diphosphatase (EC 3.6.1.1) from Rhipicephalus microplus, also shows exopolyphosphatase activity. It has a greater affinity, higher catalytic efficiency and increased cooperativity for sodium phosphate glass type 15 (polyP15) than for sodium tripolyphosphate (polyP3). Molecular docking study. PolyP3 binds close to the Mg2+ atoms in the catalytic region of the protein, participating in their coordination network, whereas polyP15 interactions involve negatively charged phosphate groups and basic amino acid residues, such as Lys56, Arg58, and Lys193. PolyP15 has a more favourable theoretical binding affinity than polyP3, thus supporting the kinetic data
-
-
-
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
?
additional information
?
-
-
PPN1 splitting long polyphosphate chains to shorter ones
-
-
?
additional information
?
-
-
PPX1 splitting off phosphate from the end of the polyphosphate chain
-
-
?
additional information
?
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of EC 3.6.1.11 and EC 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of EC 3.6.1.11 and EC 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenylphosphate
-
-
?
additional information
?
-
Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
-
Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
?
additional information
?
-
the PPX1 does not hydrolyze organic triphosphates such as ATP, diphosphate or long-chain polyphosphates. PPX1 does not contain a cyclic-nucleotide specific phosphodiesterase activity
-
-
?
additional information
?
-
-
the PPX1 does not hydrolyze organic triphosphates such as ATP, diphosphate or long-chain polyphosphates. PPX1 does not contain a cyclic-nucleotide specific phosphodiesterase activity
-
-
?
additional information
?
-
the PPX1 does not hydrolyze organic triphosphates such as ATP, diphosphate or long-chain polyphosphates. PPX1 does not contain a cyclic-nucleotide specific phosphodiesterase activity
-
-
?
additional information
?
-
TbNH2 is an exopolyphosphatase with higher activity on short chain polyphosphates. TbNH2 can dephosphorylate ATP and ADP but with lower affinity than for polyphosphate. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). TbNH2 has a higher affinity for polyphosphate700 than for polyphosphate60. TbNH2 has activity to release the gamma and beta phosphates from ATP and ADP
-
-
-
additional information
?
-
TbNH2 is an exopolyphosphatase with higher activity on short chain polyphosphates. TbNH2 can dephosphorylate ATP and ADP but with lower affinity than for polyphosphate. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). TbNH2 has a higher affinity for polyphosphate700 than for polyphosphate60. TbNH2 has activity to release the gamma and beta phosphates from ATP and ADP
-
-
-
additional information
?
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyphosphate of various chain sizes. The enzyme has a higher affinity for polyphosphate60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
-
additional information
?
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyphosphate of various chain sizes. The enzyme has a higher affinity for polyphosphate60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
-
additional information
?
-
TbNH2 is an exopolyphosphatase with higher activity on short chain polyphosphates. TbNH2 can dephosphorylate ATP and ADP but with lower affinity than for polyphosphate. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). TbNH2 has a higher affinity for polyphosphate700 than for polyphosphate60. TbNH2 has activity to release the gamma and beta phosphates from ATP and ADP
-
-
-
additional information
?
-
TbNH2 is an exopolyphosphatase with higher activity on short chain polyphosphates. TbNH2 can dephosphorylate ATP and ADP but with lower affinity than for polyphosphate. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). TbNH2 has a higher affinity for polyphosphate700 than for polyphosphate60. TbNH2 has activity to release the gamma and beta phosphates from ATP and ADP
-
-
-
additional information
?
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyphosphate of various chain sizes. The enzyme has a higher affinity for polyphosphate60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
-
additional information
?
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyphosphate of various chain sizes. The enzyme has a higher affinity for polyphosphate60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
-
additional information
?
-
polyphosphates play a role in the parasite's osmoregulation, overview
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-
?
additional information
?
-
-
polyphosphates play a role in the parasite's osmoregulation, overview
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-
?
additional information
?
-
the enzyme prefers short-chain polyphosphates, substrate specificity, TcPPX is a processive enzyme and does not hydrolyze ATP, diphosphate, or 4-nitrophenyl phosphate, although it hydrolyzes guanosine 5'-tetraphosphate very efficiently, overview
-
-
?
additional information
?
-
-
the enzyme prefers short-chain polyphosphates, substrate specificity, TcPPX is a processive enzyme and does not hydrolyze ATP, diphosphate, or 4-nitrophenyl phosphate, although it hydrolyzes guanosine 5'-tetraphosphate very efficiently, overview
-
-
?
additional information
?
-
recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
-
-
-
additional information
?
-
-
recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
-
-
-
additional information
?
-
recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
-
-
-
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Ca2+
-
in the presence of Ca2+, the activity is about 20% of levels with Mg2+
Cd2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
Cs+
-
activates wild-type, full-length enzyme paPpx(1-506)
Cu2+
-
0.01 mM, stimulates
NaCl
-
50 and 200 mM, 46 and 42% activity enhancement, respectively
NH4Cl
-
50 and 200 mM, 42 and 67% activity enhancement, respectively
Rb+
-
activates wild-type, full-length enzyme paPpx(1-506)
Co2+
KD: 46.9 +/- 5.66 micorM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Co2+
-
reaction requires a divalent metal cofactor
Co2+
-
little effect on polyP15 hydrolysis
Co2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Co2+
-
activates 4.4fold polyphosphatase II and activates 1.5fold polyphosphatase I both at 0.15 mM
Co2+
-
0.1 mM Co2+, PPX activity is stimulated by a factor of two in the nuclear fraction, but not in the mitochondrial fraction
Co2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Co2+
-
2 mM CoCl2, 2.5fold stimulation
Co2+
-
stimulated by divalent cations, Co2+ is the best stimulator, 6fold at 0.05 mM
Co2+
-
5 mM, 108% of the activation by Mg2+
Co2+
-
6fold activation at 0.1 mM
Co2+
0.1 mM, 31fold activity enhancement
Co2+
-
0.1 mM, 6fold activity stimulation
Co2+
-
2.5fold activation
Co2+
best activator, maximum activation at 0.1 mM
Co2+
Co2+ stimulates phosphate release from the polyphosphate chain end
Fe2+
enzyme is stimulated 0.26fold at a concentration of 2 mM
Fe2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Fe2+
-
5 mM, 34% of the activation by Mg2+
K+
20 mM, about 3fold stimulation
K+
PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity
K+
-
activates 2fold polyphosphatase II, but not activates polyphosphatase I
K+
-
a nonessential activator of paPpx, presence of K+ does not affect the affinity of the enzyme for Mg2+, activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with K+ is sigmoid and reaches its maximum activity at concentrations of 80 mM. Km(app)K+ is 42 mM
K+
100 mM, 30% activity enhancement
KCl
-
175 mM, stimulates
KCl
-
50 and 200 mM, 39 and 38% activity enhancement, respectively
Mg2+
best activator, maximum activity at 5 mM
Mg2+
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
Mg2+
-
divalent cation required, Mg2+ is most effective
Mg2+
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ with 5'-AMP
Mg2+
-
reaction requires a divalent metal cofactor, bound substrate enhances enzyme affinity for the metal ion
Mg2+
-
best activator at 1 mM using polyP3, polyP4 and polyP15 as substrates
Mg2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mg2+
may partly substitute for Mn2+
Mg2+
-
the activity of NMB1467 is dependent on Mg2+ with optimal activity observed with between 1 and 2 mM
Mg2+
-
required, values of 0.5(app)Mg2+ in paPpx(1-506) and NpaPpx(1-314) are 0.30 mM and 0.28 mM, respectively. The interaction between paPpx(1-506) and Mg2+ occurs in the N-terminal domain
Mg2+
-
2.5 mM Mg2+, PPX activity is stimulated by a factor of two in the nuclear fraction and in the mitochondrial fraction
Mg2+
-
required, family I diphosphatases are Mg2+-dependent, activates
Mg2+
about 50% of the activity with Mn2+
Mg2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
-
1-10 mM, about 7fold activation
Mg2+
-
required, optimal activity at 5 mM
Mg2+
-
2fold activation at 0.1 mM
Mg2+
-
0.1 mM MgSO4, 5% activity loss
Mg2+
-
1 mM, 2fold activity enhancement
Mg2+
2.5 mM, 15fold activity enhancement
Mg2+
-
1.6fold activation
Mg2+
-
single tight binding site for Mg2+
Mg2+
-
optimal activity of exopolyphosphatase II in presence of 3 mM
Mg2+
activates, preferred divalent cation
Mn2+
5 mM, about 37% of the activity with Mg2+
Mn2+
5 mM, about 65% of the activity with Mg2+
Mn2+
enzyme is stimulated 0.86fold at a concentration of 2 mM
Mn2+
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
Mn2+
-
reaction requires a divalent metal cofactor, Mn2+ confers 50% activity compared to Mg2+ in P3 and P4 hydrolysis
Mn2+
-
best activator for guanosine 5'-tetraphosphate hydrolysis
Mn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mn2+
required, optimum concentration 1 mM
Mn2+
preferred divalent cation, required. Optimal concentration about 10 mM
Mn2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
1-10 mM, 3-5fold stimulation
Mn2+
-
0.5 mM, stimulates
NH4+
-
activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with NH4+ is sigmoid and reaches its maximum activity at concentrations of 30 mM. Km(app)NH4+ is 10 mM
NH4+
100 mM, 35% activity enhancement
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
Ni2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Ni2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
-
5 mM, 32% of the activation by Mg2+
Zn2+
enzyme is stimulated 0.11fold at a concentration of 2 mM
Zn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Zn2+
may partly substitute for Mn2+
Zn2+
-
Zn2+ is able to activate the enzyme only 20% compared to Mg2+
Zn2+
-
1.5fold activation at 0.1 mM
Zn2+
-
0.1 mM ZnSO4, 76% activity loss
Zn2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
additional information
presence of divalent cation is absolutely required, Mg2+ is preferred
additional information
presence of divalent cation is absolutely required, Mg2+ is preferred
additional information
-
no activity measured in absence of divalent cations
additional information
no activity with Ca2+, Co2+, Cu2+ or Fe2+ ions
additional information
-
no activity with Ca2+, Co2+, Cu2+ or Fe2+ ions
additional information
-
behavior of the full-length paPpx(1-506) and N-paPpx(1-314) against different concentration of divalent ions such as Mg2+, Zn2+, Ca2+, and Mn2+ as effectors, in presence of a saturating concentration (0.008 mM) for the substrate polyphosphate65. The activation of both enzyme variants by Mg2+ is similar and shows no inhibition at high concentrations of this ion. The activation by Ca2+ and Mn2+ is negligible. Li+ and Na+ have no effects on enzyme activity, while NH4+, K+, Rb+, and Cs+ are activators of paPpx(1-506). Tetramethylammonium is not an activator of paPpx(1-506)
additional information
-
no effect on activity by Mn2+ and Zn2+
additional information
-
stimulated by divalent cations to a lesser extent
additional information
-
exopolyphosphatase I does not require divalent cations
additional information
enzyme TbNH2 is able to hydrolyze polyphosphate with Mg2+ and Co2+ as cofactors, but has lower activity with Mn2+
additional information
enzyme TbNH2 is able to hydrolyze polyphosphate with Mg2+ and Co2+ as cofactors, but has lower activity with Mn2+
additional information
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+
additional information
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+
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0.025 - 0.133
(25R)-3beta-hydroxycholest-5-en-27-oate
0.264 - 0.597
(phosphate)13-18
-
0.0011 - 0.0028
(phosphate)15
0.0069
(phosphate)25
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.0002 - 0.213
(phosphate)3
0.019 - 0.041
(phosphate)4
0.0022
(phosphate)45
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.0007 - 0.0036
(phosphate)65
-
0.0173
(polyphosphate)130
pH 6.8, 37°C
-
0.0059
(polyphosphate)14
pH 6.8, 37°C
-
0.0121
(polyphosphate)60
pH 6.8, 37°C
-
0.0035 - 1343
(Polyphosphate)n
0.028 - 0.08
adenosine 5'-tetraphosphate
0.1
adenosine-5'-tetraphosphate
-
-
0.0465
ADP
pH 7.4, 37°C, recombinant enzyme
0.0781
ATP
pH 7.4, 37°C, recombinant enzyme
0.0033
cAMP
pH 7.2, 30°C, recombinant enzyme
0.012 - 54.5
guanosine 5'-tetraphosphate
0.08
guanosine-5'-tetraphosphate
-
-
2.49
p-nitrophenyl phosphate
+/- 0.4
0.0272
pentasodium triphosphate
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30°C
0.0035 - 12
Polyphosphate
75
polyphosphate 15
-
-
-
3.5
polyphosphate 208
-
-
-
1100
polyphosphate 3
-
-
-
0.3315
polyphosphate glass type 15
-
recombinant enzyme, pH 7.5, 30°C
-
0.01103 - 0.02083
polyphosphate25
0.7244
polyphosphate3
-
recombinant enzyme, pH 7.5, 30°C
-
0.00714 - 0.0236
polyphosphate45
-
0.0822 - 0.2005
polyphosphate60
-
0.00329 - 0.02517
polyphosphate65
-
0.1256 - 0.1494
polyphosphate700
-
0.0013 - 0.03067
polyphosphate75
-
0.0022
sodium phosphate glass type 15
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28°C
-
0.11
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.0002 - 0.058
Triphosphate
0.14 - 0.41
tripolyphosphate
additional information
additional information
-
0.025
(25R)-3beta-hydroxycholest-5-en-27-oate
polyphosphate 208, in the presence of 2.5 mM Mg2+
0.133
(25R)-3beta-hydroxycholest-5-en-27-oate
polyphosphate 15, in the presence of 2.5 mM Mg2+
0.264
(phosphate)13-18
pH 6.5, 25°C
-
0.597
(phosphate)13-18
pH 6.5, 25°C
-
0.0011
(phosphate)15
-
nuclear fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
0.0028
(phosphate)15
-
mitochondrial fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
0.0002
(phosphate)3
-
mitochondrial fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
0.0007
(phosphate)3
-
nuclear fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
0.0012
(phosphate)3
-
D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0022
(phosphate)3
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0026
(phosphate)3
-
H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0066
(phosphate)3
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.015
(phosphate)3
-
H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.046
(phosphate)3
-
R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0977
(phosphate)3
pH 6.5, 25°C
0.213
(phosphate)3
pH 6.5, 25°C
0.019
(phosphate)4
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.041
(phosphate)4
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0007
(phosphate)65
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.0009
(phosphate)65
-
nuclear fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
-
0.0036
(phosphate)65
-
mitochondrial fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5
-
0.0035
(Polyphosphate)n
-
n = 208, pH 7.2, 30°C
0.02
(Polyphosphate)n
+/- 0.003
0.025
(Polyphosphate)n
n = 208
0.075
(Polyphosphate)n
-
n = 15, pH 7.2, 30°C
0.133
(Polyphosphate)n
n = 15
1.1
(Polyphosphate)n
-
n = 3, pH 7.2, 30°C
26.8
(Polyphosphate)n
-
n = 4, pH 7.2
28.1
(Polyphosphate)n
-
n = 3, pH 7.2
39.1
(Polyphosphate)n
-
n = 15, pH 7.2
57.6
(Polyphosphate)n
-
n = 75, pH 7.2
1343
(Polyphosphate)n
-
n = 45, pH 7.2
0.028
adenosine 5'-tetraphosphate
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.037
adenosine 5'-tetraphosphate
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.08
adenosine 5'-tetraphosphate
-
at pH 4.8, 50 mM sodium acetate, 5 mM CoCl2
0.012
guanosine 5'-tetraphosphate
pH 7.5, 30°C
0.041
guanosine 5'-tetraphosphate
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.099
guanosine 5'-tetraphosphate
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.242
guanosine 5'-tetraphosphate
pH 6.5, 25°C
0.335
guanosine 5'-tetraphosphate
pH 6.5, 25°C
54.5
guanosine 5'-tetraphosphate
-
pH 7.2
0.0039
polyP10
-
-
0.0092
polyP10
-
exopolyphosphatase II
0.0238
polyP10
-
exopolyphosphatase I
0.011
polyP15
-
-
0.0012
polyP208
-
-
0.0035
Polyphosphate
-
208 phosphate residues, pH 7.2
0.075
Polyphosphate
-
15 phosphate residues, pH 7.2
1.1
Polyphosphate
-
3 phosphate residues, pH 7.2
5
Polyphosphate
-
pH 7.2, 25°C, recombinant wild-type enzyme
6
Polyphosphate
-
pH 7.2, 25°C, recombinant mutant H149N
7.5
Polyphosphate
-
pH 7.2, 25°C, recombinant mutant H148N
9
Polyphosphate
-
pH 7.2, 25°C, recombinant mutant N35H
12
Polyphosphate
-
pH 7.2, 25°C, recombinant mutant D127N
0.01103
polyphosphate25
-
pH 8.0, 37°C, full-length enzyme
0.02083
polyphosphate25
-
pH 8.0, 37°C, truncated enzyme
0.00714
polyphosphate45
-
pH 8.0, 37°C, full-length enzyme
-
0.0236
polyphosphate45
-
pH 8.0, 37°C, truncated enzyme
-
0.0822
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
0.2005
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
0.00329
polyphosphate65
-
pH 8.0, 37°C, full-length enzyme
-
0.02517
polyphosphate65
-
pH 8.0, 37°C, truncated enzyme
-
0.1256
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.1494
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.0013
polyphosphate75
-
pH 8.0, 37°C, full-length enzyme
-
0.03067
polyphosphate75
-
pH 8.0, 37°C, truncated enzyme
-
0.0002
Triphosphate
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28°C
0.04
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.058
Triphosphate
pH 7.5, 30°C
0.14
tripolyphosphate
-
-
0.39
tripolyphosphate
-
-
0.41
tripolyphosphate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
steady-state kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic analysis of recombinant wild-type and truncated mutant enzymes, exopolyphosphatase activity and polyphosphate:ADP phosphotransferase activity (EC 2.7.4.), overview
-
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0.006
-
strain CRX with inactivated ppx1 and ppN1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.01
-
strain CRX with inactivated ppx1 and ppN1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.014
-
40-kDa-exopolyphosphatase from Saccharomyces cerevisiae strain CRN grown on glucose
0.035
-
high-molecular weight exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.05
1.25 mM polyphosphate 3 as substrate, in the presence of 2.5 mM Mg2+
0.055
-
strain CRX with inactivated ppx1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.058
-
soluble form of exopolyphospatase from Saccharomyces cerevisiae strain CRX grown on lactate
0.07
-
strain CRX with inactivated ppn1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.097
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.119
-
soluble form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.12
wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
0.136
-
40-kDa-exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.18
-
parent strain CRY, cytosol preparation in exponential growth phase in phosphate-rich medium
0.21
0.13 mM polyphosphate 15 as substrate, in the presence of 1 mM Co2+
0.23
0.13 mM polyphosphate 15 as substrate, in the presence of 0.1 mM Co2+
0.28
0.01 mM polyphosphate 208 as substrate, in the presence of 1 mM Co2+
0.3
2.0 mM polyphosphate 208 as substrate, in the presence of 0.1 mM Co2+
0.43
overexpression of ppx1 increase the specific activity of exopolyphosphatase by 4fold compared to that of the empty vector control
0.47
-
enzyme from cystosol
0.8
crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1
1.11
-
after ammonium sulfate precipitation
1.26
-
mitochondrial fraction
126
substrate (phosphate)300, pH 6.5, 25°C
15
substrate (phosphate)300, pH 6.5, 25°C
170
substrate (phosphate)13-18, pH 6.5, 25°C
180
substrate (phosphate)13-18, pH 6.5, 25°C
2070
-
purified recombinant enzyme
290
substrate (phosphate)208, presence of 0.1 mM Co2+, pH 7.2, 30°C
3 - 8
substrate (phosphate)3, presence of 0.1 mM Co2+, pH 7.2, 30°C
5
-
after DEAE-Toyopearl 650 M column chromatography
590
substrate (phosphate)3, pH 6.5, 25°C
7.24
+/- 0.34, p-nitrophenyl phosphate
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRX grown on lactate
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.04
analysis of the constructed deletion mutant ppx2 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
0.04
1.25 mM diphosphate as substrate, in the presence of 2.5 mM Mg2+
0.04
-
strain CRX with inactivated ppx1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.08
analysis of the constructed deletion mutant ppx1 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
0.08
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.095
0.01 mM polyphosphate 208 as substrate, in the presence of 2.5 mM Mg2+
0.095
-
strain CRX with inactivated ppn1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.1
+/- 0.01, polyphosphate
0.1
0.13 mM polyphosphate 15 as substrate, in the presence of 2.5 mM Mg2+
0.1
-
parent strain CRY, cytosol preparation in exponential growth phase in phosphate-deficient medium
150
-
pH 7.2, 30°C, polyP208 as substrate
150
-
after 319fold purification with heparin agarose, at 30°C in 1 ml of reaction mixture containing 50 mM Tris-HCl buffer, pH 7.2, 0.1 mM CoSO4, 200 mM ammonium chloride, and 0.01 mM polyphosphate 208
240
substrate (phosphate)15, presence of 0.1 mM Co2+, pH 7.2, 30°C
240
purified recombinant enzyme, pH 7.2, 30°C
additional information
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
additional information
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
additional information
-
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
additional information
-
-
additional information
-
h-prune efficiently hydrolyzes short-chain polyphosphates, including inorganic tripoly- and tetrapolyphosphates and nucleoside 5'-tetraphosphates, long-chain inorganic polyphosphates (more than 25 phosphate residues) are converted more slowly
additional information
-
increasing amounts of total RNA extracted from eggs progressively enhance nuclear PPX activity, whereas it exerts no effect on mitochondrial PPX activity, nuclear PPX activity increases throughout embryogenesis
additional information
-
-
additional information
-
-
additional information
-
the exopolyphosphatase activity is reduced 6.5fold in the mutant CRN lacking endopolyphosphatase activity
additional information
-
no specific activity on diphosphate, ATP and p-nitrophenyl phosphate
additional information
-
polyphosphate levels in different cell compartments, overview
additional information
-
polyphosphate hydrolysis in the CRX strain cytosol completes in 120 min
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evolution
the enzyme belongs to the DHH family of phosphoesterases. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast
evolution
the enzyme belongs to the PPX/GppA phosphatase family (pfam02541) that consists of PPX (EC 3.6.1.11) and guanosine pentaphosphate phosphohydrolase (GppA, EC 3.6.1.40) enzymes
evolution
the exopolyphosphatase belongs to the ASKHA protein superfamily
evolution
the Nudix superfamily (Pfam PF00293) is found in archaea, bacteria, eukaryotes and viruses and includes pyrophosphohydrolases of nucleotide sugars and alcohols, nucleoside and deoxynucleoside triphosphates ([d]NTPs), dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. Trypanosoma brucei has five Nudix hydrolases
evolution
-
the enzyme belongs to the DHH family of phosphoesterases. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast
-
evolution
-
the enzyme belongs to the PPX/GppA phosphatase family (pfam02541) that consists of PPX (EC 3.6.1.11) and guanosine pentaphosphate phosphohydrolase (GppA, EC 3.6.1.40) enzymes
-
evolution
-
the Nudix superfamily (Pfam PF00293) is found in archaea, bacteria, eukaryotes and viruses and includes pyrophosphohydrolases of nucleotide sugars and alcohols, nucleoside and deoxynucleoside triphosphates ([d]NTPs), dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. Trypanosoma brucei has five Nudix hydrolases
-
malfunction
-
bacteria lacking PPX exhibit increased resistance to complement-mediated killing. Loss of PPX leads to decrease in alternative pathway activation on bacterial surface
malfunction
PPX1 genetic ablation does not produce a dramatic phenotype
malfunction
deficiency of exopolyphosphatase results in decelerated growth during logarithmic-phase in axenic cultures, and tolerance to the cell wall-active drug isoniazid. The enzyme-deficient mutant shows a significant survival defect in activated human macrophages and reduced persistence in the lungs of guinea pigs
malfunction
analysis of single ppx- or ppk- mutants and of the double mutant, demonstrate a relationship between these genes and the survival capacity
malfunction
-
PPX1 genetic ablation does not produce a dramatic phenotype
-
malfunction
-
deficiency of exopolyphosphatase results in decelerated growth during logarithmic-phase in axenic cultures, and tolerance to the cell wall-active drug isoniazid. The enzyme-deficient mutant shows a significant survival defect in activated human macrophages and reduced persistence in the lungs of guinea pigs
-
metabolism
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
metabolism
polyphosphate kinase (PPK) is the principal source of polyphosphate in most bacteria, whereas exopolyphosphatases (PPX) are mainly responsible for the degradation of polyphosphate
metabolism
the enzyme PPN1 shows only exopolyphosphatase activity
metabolism
-
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
-
metabolism
-
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
-
metabolism
-
the enzyme PPN1 shows only exopolyphosphatase activity
-
metabolism
-
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
-
metabolism
-
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
-
metabolism
-
inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348. Existence of a polyphosphate-dependent copper-resistance system that may be of great importance in the adaptation of this thermoacidophilic archaeon to its harsh environment
-
metabolism
-
polyphosphate kinase (PPK) is the principal source of polyphosphate in most bacteria, whereas exopolyphosphatases (PPX) are mainly responsible for the degradation of polyphosphate
-
physiological function
-
the biochemical activity of PPX is necessary for interactions with the complement
physiological function
-
exopolyphosphatase activity is regulated during mitochondrial respiration and plays a role in adenosine-5-triphosphate synthesis in hard tick embryos
physiological function
exopolyphosphatase is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
physiological function
deletion mutants of exopolyphosphatases Ppx1, Ppx2 and the double knockout mutant all exhibit increased capacity to accumulate polyphosphate. Ppx1 and double mutants show decreased accumulation of ppGpp, an alarmone molecule. The lack of ppx gene products results in defects in motility, biofilm formation, nutrient stress survival, invasion and intracellular survival indicating that maintaining a certain level of polyphosphate is critical for Ppx genes in Campylobacter jejuni pathophysiology. Both Ppx1 and Ppx2 mutants are resistant to human complement-mediated killing. The double mutant mutant is sensitive. The serum susceptibility does not occur in the presence of MgCl2 and EGTA. The chicken serum does not have any effect on the mutants' survival. The observed serum susceptibility is not related to surface capsule and lipooligosaccharide structures
physiological function
double deletion mutants of exopolyphosphatases Ppx1/Ppx2 and the double knockout mutant all exhibit increased capacity to accumulate polyphosphate. Ppx1 and double mutants show decreased accumulation of ppGpp, an alarmone molecule. The lack of ppx gene products results in defects in motility, biofilm formation, nutrient stress survival, invasion and intracellular survival indicating that maintaining a certain level of polyphosphate is critical for Ppx genes in Campylobacter jejuni pathophysiology. Both Ppx1 and Ppx2 mutants are resistant to human complement-mediated killing. The double mutant mutant is sensitive. The serum susceptibility does not occur in the presence of MgCl2 and EGTA. The chicken serum does not have any effect on the mutants' survival. The observed serum susceptibility is not related to surface capsule and lipooligosaccharide structures
physiological function
exopolyphosphatase Ppx is involved in the production of virulence factors associated with both acute infection (e.g. motility-promoting factors, blue/green pigment production, C6-C12 quorum-sensing homoserine lactones) and chronic infection (e.g. rhamnolipids, biofilm formation). Pseudomonas aeruginosa maintains consistently proper levels of Ppx regardless of environmental conditions. A mutant strain lacking Ppx activity does not grow in phosphate-deficient medium and the survival after 8 or 24 h declines by 25-30% of the initial value
physiological function
strong constitutive overexpression of exopolyphosphatase PPN1 results in 28- and 11fold increase in activity compared to the PPN1 mutant and wild-type strains, respectively. The content of acid-soluble polyphosphate decreases about 6fold and the content of acid-insoluble polyphosphate decreases about 2.5fold in the cells of the transformant compared to the mutant strain
physiological function
exopolyphosphatase (PPX) enzymes degrade inorganic polyphosphate (poly-P), which is essential for the survival of microbial cells in response to external stresses. Inorganic polyphosphate (poly-P), comprising a few to hundreds of orthophosphate residues linked by high-energy phosphoanhydride bonds, is found in virtually all living cells
physiological function
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Endopolyphosphatase (PPN) activity cleaves internal phosphoanhydride bonds generating shorter polyphosphate molecules. Nudix hydrolase 4 (TbNH4 or TbDcp2) is a mRNA de-capping enzyme that removes the 5' cap from processed mRNAs, EC 3.6.1.62
physiological function
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Hydrolysis of polyphosphate with release of phosphate occurs by the activity of a cytosolic exopolyphosphatase (PPX)
physiological function
the exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Polyphosphate plays a remarkable role in pathogenesis, survival and stress tolerance
physiological function
-
double deletion mutants of exopolyphosphatases Ppx1/Ppx2 and the double knockout mutant all exhibit increased capacity to accumulate polyphosphate. Ppx1 and double mutants show decreased accumulation of ppGpp, an alarmone molecule. The lack of ppx gene products results in defects in motility, biofilm formation, nutrient stress survival, invasion and intracellular survival indicating that maintaining a certain level of polyphosphate is critical for Ppx genes in Campylobacter jejuni pathophysiology. Both Ppx1 and Ppx2 mutants are resistant to human complement-mediated killing. The double mutant mutant is sensitive. The serum susceptibility does not occur in the presence of MgCl2 and EGTA. The chicken serum does not have any effect on the mutants' survival. The observed serum susceptibility is not related to surface capsule and lipooligosaccharide structures
-
physiological function
-
deletion mutants of exopolyphosphatases Ppx1, Ppx2 and the double knockout mutant all exhibit increased capacity to accumulate polyphosphate. Ppx1 and double mutants show decreased accumulation of ppGpp, an alarmone molecule. The lack of ppx gene products results in defects in motility, biofilm formation, nutrient stress survival, invasion and intracellular survival indicating that maintaining a certain level of polyphosphate is critical for Ppx genes in Campylobacter jejuni pathophysiology. Both Ppx1 and Ppx2 mutants are resistant to human complement-mediated killing. The double mutant mutant is sensitive. The serum susceptibility does not occur in the presence of MgCl2 and EGTA. The chicken serum does not have any effect on the mutants' survival. The observed serum susceptibility is not related to surface capsule and lipooligosaccharide structures
-
physiological function
-
exopolyphosphatase is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
-
physiological function
-
exopolyphosphatase (PPX) enzymes degrade inorganic polyphosphate (poly-P), which is essential for the survival of microbial cells in response to external stresses. Inorganic polyphosphate (poly-P), comprising a few to hundreds of orthophosphate residues linked by high-energy phosphoanhydride bonds, is found in virtually all living cells
-
physiological function
-
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Hydrolysis of polyphosphate with release of phosphate occurs by the activity of a cytosolic exopolyphosphatase (PPX)
-
physiological function
-
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Endopolyphosphatase (PPN) activity cleaves internal phosphoanhydride bonds generating shorter polyphosphate molecules. Nudix hydrolase 4 (TbNH4 or TbDcp2) is a mRNA de-capping enzyme that removes the 5' cap from processed mRNAs, EC 3.6.1.62
-
additional information
-
a homology model of paPpx in a closed conformation is constructed by comparative modeling, molecular dynamic simulations, overview. Docking study with bound metals and/or ADP defining the N-paPpx(1-314) model in open conformation as receptor. Enzyme electrostatic potential calculations
additional information
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
additional information
substrate binding structure analysis, different computational approaches, site-direct mutagenesis and kinetic data are applied to understand the relationship between structure and function of exopolyphosphatase. Enzyme residue H378 is proposed as a fundamental gatekeeper for the recognition of long chain polyphosphate. Implication of H378 protonation state, overview. Electrostatic and energy calculations and molecular docking study, molecular dynamics simulations, overview. The frontal surface of the protein has a clear predominance of electropositive potential and the minimum binding energies are also obtained in that surface. This is favored by interaction with R166,K197, H382, G380, and K414. Other favorable region is formed by residues K353, K428, K429, K430 and Q431 in the joint of domains I and IV. On the contrary, the binding energies of the back side of the protein surface are unfavorable to bind polyphosphate, consistent with a predominance of electronegative potential. Indeed, ecPpx is characterized by a clear division between electropositive (frontal) and electronegative (back) potential
additional information
-
substrate binding structure analysis, different computational approaches, site-direct mutagenesis and kinetic data are applied to understand the relationship between structure and function of exopolyphosphatase. Enzyme residue H378 is proposed as a fundamental gatekeeper for the recognition of long chain polyphosphate. Implication of H378 protonation state, overview. Electrostatic and energy calculations and molecular docking study, molecular dynamics simulations, overview. The frontal surface of the protein has a clear predominance of electropositive potential and the minimum binding energies are also obtained in that surface. This is favored by interaction with R166,K197, H382, G380, and K414. Other favorable region is formed by residues K353, K428, K429, K430 and Q431 in the joint of domains I and IV. On the contrary, the binding energies of the back side of the protein surface are unfavorable to bind polyphosphate, consistent with a predominance of electronegative potential. Indeed, ecPpx is characterized by a clear division between electropositive (frontal) and electronegative (back) potential
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
-
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
-
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
-
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
-
additional information
-
homology modeling structure modelling, Aquifex aeolicus PPX structure (PDB ID 1T6C) is used as the template, overview
-
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D143A
-
single amino acid mutation of Ppx
E121A
-
single amino acid mutation of Ppx
E150A
-
single amino acid mutation of Ppx
E371A
-
single amino acid mutation of Ppx
D106A
-
variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
D179A
-
variant is inactive
D28A
-
variant is inactive
H107N
-
variant displays reduced activity with a turnover value of 4.4% compared to the wild type counterpart, Km value increases 7fold
H108N
-
variant displays reduced activity with a turnover value of 32% compared to the wild type counterpart
N24H
-
variant is inactive
R128H
-
enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold
R348A
-
variant is inactive
E111A
site-directed mutagenesis, inactive mutant
E112A
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
E113A
site-directed mutagenesis, inactive mutant
E111A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E113A
-
site-directed mutagenesis, inactive mutant
-
D127E
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
D127N
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
H148N
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat in comparison to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
H149N
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat in comparison to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
N35H
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activation by divalent cations differs between wild-type and mutant enzymes, overview
D127E
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
-
D127N
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
-
H148N
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat in comparison to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
-
N35H
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activation by divalent cations differs between wild-type and mutant enzymes, overview
-
E137A
site-directed mutagenesis of the truncated mutant ZmPPX(30-508), an active site mutant
E137A
-
site-directed mutagenesis of the truncated mutant ZmPPX(30-508), an active site mutant
-
additional information
-
construction of a truncated enzyme mutants comprising amino acid residues 1-314 of 506 (N-paPpx(1-314)), or residues 1-303 (N-paPpx(1-303)), or residues 315-506 (C-paPpx(315-506)) of paPpx, amplified from Pseudomonas aeruginosa wild-type strain PAO1 chromosomal DNA through PCR. Only paPpx(1-506) and N-paPpx(1-314) are enzymatically active, while C-paPpx(315-506) lacks enzymatic activity
additional information
-
inactivation of PPN1 affects the polyP level in the nuclei insignificantly in the stationary phase, while in the exponential phase the level increases 2.3fold as compared with the parent strain of Saccharomyces cerevisiae, overview
additional information
-
inactivation of the PPX1 gene has no effect on the polyP metabolism under cultivation of the yeast in medium with glucose and phosphate, while inactivation of the PPN1 gene results in elimination of the high-molecular-mass exopolyphosphatases of the cytosol, nuclei, vacuoles, and mitochondria of Saccharomyces cerevisiae, PPN1 inactivation has negligible effect on polyP levels, it results in increase in the long-chain polyPs in all the compartments under study
additional information
-
mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme
additional information
construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels
additional information
-
construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels
additional information
-
mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme
-
additional information
-
construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels
-
additional information
-
inactivation of the PPX1 gene has no effect on the polyP metabolism under cultivation of the yeast in medium with glucose and phosphate, while inactivation of the PPN1 gene results in elimination of the high-molecular-mass exopolyphosphatases of the cytosol, nuclei, vacuoles, and mitochondria of Saccharomyces cerevisiae, PPN1 inactivation has negligible effect on polyP levels, it results in increase in the long-chain polyPs in all the compartments under study
-
additional information
overexpression of PPX results in a dramatic decrease in total short-chain polyphoaphates and partial decrease in long-chain polyphosphates accompanied by a delayed regulatory volume decrease after hyposmotic stress, overview
additional information
-
overexpression of PPX results in a dramatic decrease in total short-chain polyphoaphates and partial decrease in long-chain polyphosphates accompanied by a delayed regulatory volume decrease after hyposmotic stress, overview
additional information
truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
additional information
-
truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
additional information
-
truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
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