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Information on EC 3.6.1.11 - exopolyphosphatase
for references in articles please use BRENDA:EC3.6.1.11
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.11 exopolyphosphatase
The enzyme appears in viruses and cellular organisms
showSynonyms
exopolyphosphatase, polyphosphate phosphatase, polyphosphate phosphohydrolase, exopolypase, rv0496, exopoly(p)ase, pappx, high molecular weight exopolyphosphatase, exopolyphosphatase 1, lmppx, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
40 kD exopolyphosphatase
acid phosphoanhydride phosphohydrolase
-
-
-
-
CJJ81176_0377
CJJ81176_1251
CT0099
CT1713
exopoly(P)ase
-
-
-
-
ExopolyPase
exopolyphosphatase
Gra-Pase
-
-
-
-
high molecular mass exopolyphosphatase
high molecular weight exopolyphosphatase
major cytosolic exopolyphosphatase PPX1
metaphosphatase
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-
-
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Msed_0981
MT0516
MXAN_5759
MXAN_6322
nuclear exopolyphosphatase
Nudix hydrolase
phosphatase, exopoly-
-
-
-
-
polyphosphate phosphohydrolase
polyphosphate-phosphohydrolase
Ppn1
PPX
Ppx/GppA phosphatase
PPX1
PPX2
PPXMsed
Rv0496
Rv1026
Tb927.5.4350
Tb927.6.2670
TbDcp2
TbNH2
TbNH4
YHR201C
Za10_0559
ZmPPX
additional information
ExopolyPase
-
-
-
-
additional information
-
PPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase, PPase
additional information
-
PPX1 belongs to the DHH family of phosphoesterases
additional information
-
PPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase, PPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
the interaction of the enzyme with polyphosphate is independent on cation concentration, binding is not driven by entropy from release of polyelectrolyte condensed cations
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(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
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(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
hydrolyzes poly-phosphates with an average chain length of 208 to 15 phosphate residues
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(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
hydrolyzes poly-phosphates with an average chain length of 208 to 15 phosphate residues
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
phosphorous acid anhydride hydrolysis
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-
-
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9024-85-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(phosphate)9 + H2O
(phosphate)8 + phosphate
Substrates: 45% of the activity with (phosphate)25
Products: -
Products: -
?
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
Substrates: -
Products: -
Products: -
?
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
-
Substrates: -
Products: -
Products: -
?
inosine tetraphosphate + H2O
ITP + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
polyP15 + H2O
polyP14 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyP208 + H2O
polyP207 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate + H2O
?
-
Substrates: chain length of more than 45 phosphate residues
Products: -
Products: -
?
polyphosphate 188 + H2O
polyphosphate 187 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 75 + H2O
polyphosphate 74 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate45 + H2O
polyphosphate44 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate75 + H2O
polyphosphate74 + phosphate
-
Substrates: -
Products: -
Products: -
?
sodium phosphate glass type 15 + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
Substrates: -
Products: -
Products: -
?
(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
-
Substrates: -
Products: -
Products: -
?
(phosphate)13-18 + H2O
(phosphate)12-17 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)13-18 + H2O
(phosphate)12-17 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
-
Substrates: -
Products: -
Products: -
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
Substrates: 88% of the activity with (phosphate)25
Products: -
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?
(phosphate)15 + H2O
(phosphate)14 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
Substrates: 100% activity
Products: -
Products: -
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
Substrates: -
Products: reaction continues to a chain length of about 15 residues
Products: reaction continues to a chain length of about 15 residues
?
(phosphate)25 + H2O
(phosphate)24 + phosphate
Substrates: 100% activity
Products: -
Products: -
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: best substrate
Products: -
Products: -
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: best substrate
Products: -
Products: -
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: -
Products: -
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?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: 14% of the activity with (phosphate)25
Products: -
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?
(phosphate)3 + H2O
(phosphate)2 + phosphate
Substrates: -
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?
(phosphate)300 + H2O
(phosphate)299 + phosphate
Substrates: or even longer chain length
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?
(phosphate)300 + H2O
(phosphate)299 + phosphate
Substrates: or even longer chain length
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?
(phosphate)45 + H2O
(phosphate)44 + phosphate
Substrates: 100% activity
Products: -
Products: -
?
(phosphate)65 + H2O
(phosphate)64 + phosphate
-
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
Substrates: degradation of polyphosphate
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: h-prune efficiently hydrolyzes short-chain polyphosphates
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Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: regulatory enzyme in polyphosphate metabolism
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: 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
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)130 + H2O
(polyphosphate)129 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)130 + H2O
(polyphosphate)129 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)14 + H2O
(polyphosphate)13 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)14 + H2O
(polyphosphate)13 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)60 + H2O
(polyphosphate)59 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)60 + H2O
(polyphosphate)59 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: phosphate starvation induces the formation of the enzyme
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
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Substrates: enzyme is derepressed under phosphate starvation conditions
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: n = 500
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: no acyivity if n = 200
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: n = 40, 72, 180 or 290, highest reaction rate, when n is 40
Products: -
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: polyphosphatase I shows optimal activity when n is 25 phosphate residues, polyphosphatases II prefers substrates with 9 residues
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
ir
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: n = 500 - 600
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: the activity with polyP15 is 85% of that with polyP208, the activity with polyP9 is 24% of that with polyP208
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: poly P9-10, polyP33-36
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: n = 10, 25, 50, 100, 250 or 500. n = 250 is the preferred substrate
Products: -
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?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: polyP15, polyP208
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Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: chain length of 10-200 phosphate residues
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: chain length of 10-200 phosphate residues
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: 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
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
Substrates: -
Products: -
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?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
Substrates: 7.3% of the activity with polyP208
Products: -
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?
ADP + H2O
AMP + phosphate
Substrates: -
Products: -
Products: -
?
ADP + H2O
AMP + phosphate
Substrates: -
Products: -
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?
ATP + 2 H2O
AMP + 2 phosphate
Substrates: -
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?
ATP + 2 H2O
AMP + 2 phosphate
Substrates: -
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?
cAMP + H2O
adenosine + phosphate
Substrates: -
Products: -
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?
diphosphate + H2O
2 phosphate
Substrates: only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
Products: -
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?
diphosphate + H2O
2 phosphate
Substrates: only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
Products: -
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?
GTP + H2O
GDP + phosphate
Substrates: -
Products: -
Products: -
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
Substrates: -
Products: -
Products: -
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
Substrates: -
Products: -
Products: -
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
polyP10-15 + H2O
polyP9-14 + phosphate
Substrates: poor substrate
Products: -
Products: -
?
polyP10-15 + H2O
polyP9-14 + phosphate
Substrates: poor substrate
Products: -
Products: -
?
polyP17 + H2O
polyP16 + phosphate
Substrates: -
Products: -
Products: -
?
polyP17 + H2O
polyP16 + phosphate
Substrates: -
Products: -
Products: -
?
polyP60-70 + H2O
polyP59-69 + phosphate
Substrates: -
Products: -
Products: -
?
polyP60-70 + H2O
polyP59-69 + phosphate
Substrates: -
Products: -
Products: -
?
polyP700-1000 + H2O
polyP699-999 + phosphate
Substrates: -
Products: -
Products: -
?
polyP700-1000 + H2O
polyP699-999 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
Substrates: -
Products: -
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?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
Substrates: -
Products: -
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?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
Substrates: -
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Products: -
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate130 + H2O
polyphosphate129 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate130 + H2O
polyphosphate129 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate208 + H2O
?
Substrates: -
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?
polyphosphate25 + H2O
polyphosphate24 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate25 + H2O
polyphosphate24 + phosphate
-
Substrates: -
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?
polyphosphate3 + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate3 + H2O
diphosphate + phosphate
Substrates: -
Products: -
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?
polyphosphate3 + H2O
diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate60 + H2O
polyphosphate59 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate60 + H2O
polyphosphate59 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate65 + H2O
polyphosphate64 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate65 + H2O
polyphosphate64 + phosphate
-
Substrates: -
Products: -
Products: -
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
Substrates: -
Products: -
Products: -
?
polyphosphate700 + H2O
polyphosphate699 + phosphate
Substrates: -
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?
tetraphosphate + H2O
triphosphate + phosphate
Substrates: -
Products: -
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?
tetraphosphate + H2O
triphosphate + phosphate
Substrates: -
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Products: -
?
tetraphosphate + H2O
triphosphate + phosphate
Substrates: -
Products: -
Products: -
?
tetraphosphate + H2O
triphosphate + phosphate
Substrates: -
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?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
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?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
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?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
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triphosphate + H2O
diphosphate + phosphate
Substrates: -
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?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
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?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: -
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?
tripolyphosphate + H2O
phosphate + ?
-
Substrates: -
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?
tripolyphosphate + H2O
phosphate + ?
-
Substrates: 7.3% of the activity with polyP208
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?
additional information
?
-
Substrates: isoform Ppx1 shows substantial nucleoside triphosphatase activity
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?
additional information
?
-
Substrates: isoform Ppx1 shows substantial nucleoside triphosphatase activity
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Products: -
?
additional information
?
-
Substrates: isoform Ppx1 shows substantial nucleoside triphosphatase activity
Products: -
Products: -
?
additional information
?
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Substrates: isoform Ppx1 shows substantial nucleoside triphosphatase activity
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?
additional information
?
-
Substrates: PPX2 is active with short-chain polyphosphates, even accepting diphosphate
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?
additional information
?
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Substrates: PPX2 is active with short-chain polyphosphates, even accepting diphosphate
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?
additional information
?
-
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Substrates: PPX2 is active with short-chain polyphosphates, even accepting diphosphate
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?
additional information
?
-
-
Substrates: contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no expolyphosphatase against long-chain polyphosphates P45, P65 and P700
Products: -
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-
additional information
?
-
-
Substrates: ATP, diphosphate and p-nitrophenyl phosphate are not substrates
Products: -
Products: -
?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
Products: -
?
additional information
?
-
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
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?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
Products: -
?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
Products: -
?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
Products: -
?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
Products: -
?
additional information
?
-
Substrates: the purified recombinant enzyme hydrolyzes polyphosphate, E111 and E113 are essential residues for catalysis of PPXMsed
Products: -
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?
additional information
?
-
Substrates: the enzyme does not cleave ppGpp
Products: -
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?
additional information
?
-
-
Substrates: the enzyme does not cleave ppGpp
Products: -
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?
additional information
?
-
Substrates: no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
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?
additional information
?
-
-
Substrates: no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
Products: -
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?
additional information
?
-
Substrates: both PPX1 and PPX2 also display GTPase and ATPase activity in vitro
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Products: -
-
additional information
?
-
Substrates: both PPX1 and PPX2 also display GTPase and ATPase activity in vitro
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme does not cleave ppGpp
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: guanosine pentaphosphate. Enzyme hydrolyzes ATP and ADP, but lacks GTPase activities
Products: -
Products: -
?
additional information
?
-
Substrates: both PPX1 and PPX2 also display GTPase and ATPase activity in vitro
Products: -
Products: -
-
additional information
?
-
Substrates: both PPX1 and PPX2 also display GTPase and ATPase activity in vitro
Products: -
Products: -
-
additional information
?
-
Substrates: isoform Ppx1 shows weak hydrolysis of ATP and GTP in the absence of K+
Products: -
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-
additional information
?
-
Substrates: isoform Ppx1 shows weak hydrolysis of ATP and GTP in the absence of K+
Products: -
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additional information
?
-
Substrates: isoform Ppx2 prefers long-chain polyphosphates. Ppx2 shows weak hydrolysis of ATP and GTP in the absence of K+, and can also hydrolyze guanosine pentaphosphate in the presence of K+
Products: -
Products: -
-
additional information
?
-
Substrates: isoform Ppx2 prefers long-chain polyphosphates. Ppx2 shows weak hydrolysis of ATP and GTP in the absence of K+, and can also hydrolyze guanosine pentaphosphate in the presence of K+
Products: -
Products: -
-
additional information
?
-
Substrates: isoform Ppx1 shows weak hydrolysis of ATP and GTP in the absence of K+
Products: -
Products: -
-
additional information
?
-
Substrates: isoform Ppx1 shows weak hydrolysis of ATP and GTP in the absence of K+
Products: -
Products: -
-
additional information
?
-
Substrates: isoform Ppx2 prefers long-chain polyphosphates. Ppx2 shows weak hydrolysis of ATP and GTP in the absence of K+, and can also hydrolyze guanosine pentaphosphate in the presence of K+
Products: -
Products: -
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additional information
?
-
Substrates: isoform Ppx2 prefers long-chain polyphosphates. Ppx2 shows weak hydrolysis of ATP and GTP in the absence of K+, and can also hydrolyze guanosine pentaphosphate in the presence of K+
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: ATP, diphosphate and p-nitrophenyl phosphate are not substrates
Products: -
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?
additional information
?
-
-
Substrates: PPX1 splitting off phosphate from the end of the polyphosphate chain
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?
additional information
?
-
-
Substrates: PPN1 splitting long polyphosphate chains to shorter ones
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: 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
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?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
-
Substrates: ATP, diphosphate and p-nitrophenyl phosphate are not substrates
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: polyphosphates play a role in the parasite's osmoregulation, overview
Products: -
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?
additional information
?
-
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Substrates: polyphosphates play a role in the parasite's osmoregulation, overview
Products: -
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?
additional information
?
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Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
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Substrates: recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
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?
additional information
?
-
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Substrates: recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(phosphate)n + H2O
(phosphate)n-1 + phosphate
Substrates: degradation of polyphosphate
Products: -
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?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: h-prune efficiently hydrolyzes short-chain polyphosphates
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: regulatory enzyme in polyphosphate metabolism
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: phosphate starvation induces the formation of the enzyme
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: enzyme is derepressed under phosphate starvation conditions
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: -
Products: -
Products: -
ir
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
Substrates: 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
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?
polyphosphate60 + H2O
polyphosphate59 + phosphate
Substrates: -
Products: -
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?
polyphosphate60 + H2O
polyphosphate59 + phosphate
Substrates: -
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?
polyphosphate700 + H2O
polyphosphate699 + phosphate
Substrates: -
Products: -
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?
polyphosphate700 + H2O
polyphosphate699 + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PPX1 splitting off phosphate from the end of the polyphosphate chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: PPN1 splitting long polyphosphate chains to shorter ones
Products: -
Products: -
?
additional information
?
-
Substrates: polyphosphates play a role in the parasite's osmoregulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: polyphosphates play a role in the parasite's osmoregulation, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
Co2+
Fe2+
K+
KCl
Mg2+
Mn2+
NH4+
NH4Cl
-
50 and 200 mM, 42 and 67% activity enhancement, respectively
Ni2+
Zn2+
additional information
Co2+
KD: 46.9 +/- 5.66 micorM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
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+
-
stimulated by divalent cations, Co2+ is the best stimulator, 6fold at 0.05 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
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
Mg2+
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
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+
-
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+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
structure reveals the presence of two magnesium ions in the active site center
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+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mn2+
preferred divalent cation, required. Optimal concentration about 10 mM
Mn2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
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
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+
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+
-
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
isoform Ppx1 does not significantly depend on K+
additional information
isoform Ppx1 does not significantly depend on K+
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
-
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+
additional information
the phosphatase activity of PPX is strictly dependent on the presence of divalent metal cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arginine
inhibition of the recombinant enzyme at high concentrations
CaCl2
3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
dipyridamole
-
known inhibitor of phosphodiesterase, no effect on the triphosphate hydrolyzing activity of h-prune
long-chain polyphosphate
-
potential physiological regulator, inhibits h-prune-catalyzed hydrolysis of triphosphate
-
Mn2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2
nm23-H1
-
metastasis suppressor protein, the exopolyphosphatase activity is suppressed
-
polyP3
inhibits the exopolyphosphatase activity of Ppx1 toward polyP3
-
polyP700-1000
inhibits the exopolyphosphatase activity of Ppx1 toward polyP3
-
Polyphosphate
-
polyP15, 50% inhibition at 200fold polymer molar excess over the long-chain polyphosphate substrate
Pyrophosphate
8.2 mM pyrophosphate leads to half-maximal inhibition of His-tagged PPX2
Tetrapolyphosphate
-
50% inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
diphosphate
inhibits the exopolyphosphatase activity of Ppx2 toward polyP60-70 and polyP700-1000
EDTA
-
45% inhibition of polyphosphatase I and 55% inhibition of polyphosphatase II, both at 0.3 mM
heparin
-
complete inhibition of polyphosphatase I at 0.05 mg/ml, 35% inhibition of polyphosphatase II at 0.1 mg/ml
heparin
-
heparin (0.02 mg/ml) inhibits nuclear and mitochondrial PPX activity in about 90 and 95%
heparin
20 mg/l, 85% activity loss; 85% inhibition at 0.02 mg /ml
heparin
-
1 mg/l 65% activity loss, 10 mg/l 95% activity loss; 95% inactivation at 0.01 mg /ml
heparin
inhibits the endopolyphosphatase activity by 50% at 0.05 mg/ml
Mg2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 10 mM MnCl2
Mg2+
-
0.05 mM, 30% inhibition in a reaction mixture containing Co2+ at its optimal concentration
NaCl
-
600 mM NaCl, 73% inhibition of exopolyphosphatase I and 84% inhibition of exopolyphosphatase II
tripolyphosphate
-
weak inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
Zn2+
-
0.05 mM, 71% inhibition in a reaction mixture containing Co2+ at its optimal concentration
additional information
-
nucleoside triphosphates, diadenosine hexaphosphate, cAMP and dipyridamole do not affect the activity
-
additional information
not inhibited by 1 mM sodium fluoride
-
additional information
-
not inhibited by antibodies suppressing the activity of 40 kDa-exopolyphosphatase
-
additional information
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity. ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
-
additional information
-
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity. ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
-
additional information
PPX1 is not inhibited by Ro-20-1724, sildenafil, zaprinast, papaverine or etazolate, or the sodium salts of vanadate, fluoride or sulfate
-
additional information
-
PPX1 is not inhibited by Ro-20-1724, sildenafil, zaprinast, papaverine or etazolate, or the sodium salts of vanadate, fluoride or sulfate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonium chloride
200 mM, stimulates almost twofold in the presence and absence of 0.1 mM Co2+
additional information
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
-
additional information
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
-
additional information
-
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
-
additional information
-
nuclear polyphosphates decrease and activity of exopolyphosphatase increases after embryo cellularization until the end of embryogenesis
-
additional information
-
RNA does not alter the nuclear exopolyphosphatase activity
-
additional information
RNA does not alter the nuclear exopolyphosphatase activity
-
additional information
the activity of PPX1 is not affected by cAMP, deoxynucleoside triphosphates, ATP, sodium diphosphate, L-arginine, or by long polyanions such as heparin or RNA
-
additional information
-
the activity of PPX1 is not affected by cAMP, deoxynucleoside triphosphates, ATP, sodium diphosphate, L-arginine, or by long polyanions such as heparin or RNA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Catalytic properties of wheat phytase that favorably degrades long-chain inorganic polyphosphate.
Leukemia
Polyphosphate Is a Novel Pro-inflammatory Regulator of Mast Cells and Is Located in Acidocalcisomes.
Neoplasm Metastasis
Human metastasis regulator protein H-prune is a short-chain exopolyphosphatase.
Neoplasms
h-Prune is associated with poor prognosis and epithelial-mesenchymal transition in patients with colorectal liver metastases.
Neoplasms
Inositol phosphate recycling regulates glycolytic and lipid metabolism that drives cancer aggressiveness.
Starvation
Functional Insights Into the Role of gppA in (p)ppGpp Metabolism of Vibrio cholerae.
Starvation
Requirement of the exopolyphosphatase gene for cellular acclimation to phosphorus starvation in a cyanobacterium, Synechocystis sp. PCC 6803.
Tuberculosis
Deficiency of the novel exopolyphosphatase Rv1026/PPX2 leads to metabolic downshift and altered cell wall permeability in Mycobacterium tuberculosis.
Tuberculosis
Establishing Virulence Associated Polyphosphate Kinase 2 as a drug target for Mycobacterium tuberculosis.
Tuberculosis
Polyphosphate deficiency affects the sliding motility and biofilm formation of Mycobacterium smegmatis.
Tuberculosis
The role of the novel exopolyphosphatase MT0516 in Mycobacterium tuberculosis drug tolerance and persistence.
Tuberculosis
The Two PPX-GppA Homologues from Mycobacterium tuberculosis Have Distinct Biochemical Activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0069
(phosphate)25
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.0022
(phosphate)45
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.0272
pentasodium triphosphate
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30°C
0.3315
polyphosphate glass type 15
-
recombinant enzyme, pH 7.5, 30°C
-
0.0022
sodium phosphate glass type 15
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28°C
-
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+
0.0011
(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
0.019
(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
-
0.028
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
0.041
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
0.015
polyP60-70
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
0.07
polyP60-70
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
0.00181
polyP700-1000
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
0.00718
polyP700-1000
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
0.0822
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
0.2005
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
0.1256
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.1494
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.11
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.457
Tetraphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
0.613
Tetraphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
0.04
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.592
Triphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
0.68
Triphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
2.957
Triphosphate
wild-type, pH 9, 30°C, presence of Mg2+, K+
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
(phosphate)25
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.22
(phosphate)45
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.03
(phosphate)65
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
8.1
pentasodium triphosphate
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30°C
0.57
(phosphate)3
-
H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
4.2
(phosphate)3
-
H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
4.6
(phosphate)3
-
D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
19
(phosphate)3
-
R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
31
adenosine 5'-tetraphosphate
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
39
adenosine 5'-tetraphosphate
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
24
guanosine 5'-tetraphosphate
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
27
guanosine 5'-tetraphosphate
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.958
polyP60-70
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
7.083
polyP60-70
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
0.923
polyP700-1000
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
5.917
polyP700-1000
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
27.95
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
44.11
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
2.512
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
16.39
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.242
Tetraphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
0.9
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
5.25
Tetraphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
0.55
Triphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
0.6
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.705
Triphosphate
wild-type, pH 9, 30°C, presence of Mg2+, K+
5.75
Triphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.67
polyP60-70
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
466.67
polyP60-70
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
128.33
polyP700-1000
deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+
-
3333.33
polyP700-1000
wild-type, pH 9, 30°C, presence of Mg2+, K+
-
220000
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
340000
polyphosphate60
pH 7.4, 37°C, recombinant enzyme
-
20000
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
110000
polyphosphate700
pH 7.4, 37°C, recombinant enzyme
-
0.533
Tetraphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
8.5
Tetraphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
0.233
Triphosphate
wild-type, pH 9, 30°C, presence of Mg2+, K+
0.817
Triphosphate
wild-type, pH 8, 40°C, presence of Mg2+, K+
9.667
Triphosphate
fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0213
Zn2+
Trypanosoma brucei
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30°C
additional information
nm23-H1
Homo sapiens
-
2 mM Mg2+, 60 microM (phosphate)25, 10 mM triphosphate, IC50 is above 0.01 mM
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.034
0.035
-
high-molecular weight exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.04
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
0.08
0.095
0.097
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.1
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
0.8
crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1
150
240
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
additional information
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRX 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
0.13 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
-
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
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
-
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
-
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
7 - 8
7.2
7.5
6.8
highest activity of recombinant His-tagged PPX2 is reached in 50 mM PIPES buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 5.4
-
pH 4.6: 81% of maximal activity, pH 5.4: 59% of maximal activity, exopolyphosphatase I
6.2 - 8.4
-
pH 6.2: about 35% of maximal activity, pH 8.4: about 60% of maximal activity
7 - 9
-
pH 7.0: 5% of maximal activity, pH 9.0: 57% of maximal activity, exopolyphosphatase I
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 48
-
30°C: about about 60% of maximal activity, 48°C: about 40% of maximal activity
30 - 53
-
30°C: about 30% of maximal activity, 53°C: about 40% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
-
-
brenda
-
209845, 209846, 209847, 209849, 209852, 654784, 654785, 667750, 667765, 668027, 670175, 670176, 670725, 685297, 685307, 687678, 696170
-
-
brenda
bifunctional exo- and endopolyphosphatase, EC 3.6.1.11 and EC 3.6.1.10
SwissProt
brenda
bifunctional exo- and endopolyphosphatase, ECs 3.6.1.10 and 3.6.1.11
SwissProt
brenda
CRN mutant with inactive PPN1 gene, which is deficient in endopolyphosphatase activity
-
-
brenda
PPX1 mutant, two enzymes with different masses and biochemical properties
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is 134% greater in mycorrhizal roots than in non-mycorrhizal roots of Allium cepa
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
brenda
-
appears in the cytosol under PPX1 inactivation
brenda
-
nuclear exopolyphosphatase activity does not depend on the growth phase
brenda
additional information
-
no activity in the nuclear fraction
-
brenda
additional information
-
existence of 2 different PPX isoforms operating in the nuclei and mitochondria with distinct metal dependence, inhibitor and activator sensitivities
-
brenda
additional information
-
polyP metabolism in cytosol and mitochondria is substantially dependent on the carbon source, acid-soluble polyP accumulates mainly in cytosol using either glucose or ethanol. The level of the accumulation is lower during growth on ethanol compared to that on glucose. Increase in polyP content in mitochondria occurs during growth on glucose, but not on ethanol. In cytosol the activity of exopolyphosphatase PPN1 is increased and the activity of exopolyphosphatase PPX1 is decreased independently of the carbon source under phosphate surplus conditions, overview. Growth on ethanol induces exopolyphosphatase PPN1 in the soluble mitochondrial fraction, while during growth on glucose only exopolyphosphatase PPX1 is present in this fraction
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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 exopolyphosphatase belongs to the ASKHA protein superfamily
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 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 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
-
malfunction
PPX1 genetic ablation does not produce a dramatic phenotype
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
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
neurodevelopmental disorder with microcephaly, hypotonia and variable brain anomalies (NMIHBA) results from hypomorphic PRUNE1 variant alleles in humans. Two siblings who inherited missense c.383G>A; p.Arg128Gln variant from their unaffected father and a nonsense c.520G>T; p.Gly174* variant from their unaffected mother show profound developmental delay/intellectual disability, brain atrophy, seizures and absent language and, in addition, optic atrophy, esotropia, scoliosis, gastrointestinal reflux, hypotonia and spasticity
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
the enzyme PPN1 shows only exopolyphosphatase activity
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
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
-
polyphosphate kinase (PPK) is the principal source of polyphosphate in most bacteria, whereas exopolyphosphatases (PPX) are mainly responsible for the degradation of polyphosphate
-
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
-
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
-
physiological function
-
the biochemical activity of PPX is necessary for interactions with the complement
physiological function
exopolyphosphatase is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
physiological function
-
exopolyphosphatase activity is regulated during mitochondrial respiration and plays a role in adenosine-5-triphosphate synthesis in hard tick embryos
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 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
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
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
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
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
a gene disruptant mutant is similar to the wild type in the cellular content of polyphosphate an shows no defect in cell growth under phosphorus-replete conditions. Under phosphorus-starved conditions, mutant cells are defective in a phosphorus-starvation dependent decrease of polyphosphate and show deleterious phenotypes as to their survival and the stabilization of the photosystem complexes
physiological function
simultaneous deletion of both PPX1 and PPX2 strain leads to compromised biofilm formation and results in the suppression of the expression of dormancy-associated genes. Both PPX1 and PPX2 enzymes are important for Mycobacterium tuberculosis to establish infection in guinea pigs
physiological function
-
deletion of isoform Ppx1 results in bacteria unable to accumulate poly-P. Disruption of isoform Ppx2 gene does not affect poly-P synthesis. The expression of polyphosphate kinase Ppk is not altered in the Ppx1 deletion strain, and poly-P synthesis in this strain is only restored by expressing Ppx1 in trans. No poly-P synthesis is observed when Ppk is expressed from a plasmid in the Ppx1 deletion strain
physiological function
-
simultaneous deletion of both PPX1 and PPX2 strain leads to compromised biofilm formation and results in the suppression of the expression of dormancy-associated genes. Both PPX1 and PPX2 enzymes are important for Mycobacterium tuberculosis to establish infection in guinea pigs
-
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 is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
-
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
-
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
-
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
-
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
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
-
Show AA Sequence and Transmembrane Helices (5861 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
Superose 6 column gel filtration, active but unstable enzyme complex
200000
32000
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
33000
35000
40000
45000
500000
55000
33000
-
SDS-PAGE, probably a product of mRNA splicing or/and protein processing
35000
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
500000
-
Superose 6 column gel filtration, stable enzyme complex composed of two polypeptides of 32 and 35 kDa and apparently polyphosphates
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
?
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
?
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
-
dimer
two monomers form a dimer in a head to tail manner. The dimer configuration exhibits a substantial and deep aqueduct with positive potential along its interface, crystallization data
dimer
-
two monomers form a dimer in a head to tail manner. The dimer configuration exhibits a substantial and deep aqueduct with positive potential along its interface, crystallization data
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
PPN1 gene encodes a polypeptide with the predicted molecular mass of 78 kDa, the monomer molecular mass of the mature PPN1 is about 33-35 kDa
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in complex with catalytic magnesium ions and several sulfate ions. PPX contains two domains and represents a closed configuration. Four sulfate ions forming a linear dispersed chain are observed in the aqueduct of the PPX dimer
enzxme in complex with phosphate, sulfate, or ATP, X-ray diffraction structure determination and analysis at 1.6, 1.8, and 1.9 A resolution, multiple isomorphous replacement with anomalous scattering technique
-
purified recombinant detagged wild-type enzyme by hanging drop vapour diffusion, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris, pH 8.0, 500 mM NaCl, and 5% glycerol, with 0.001 ml of reservoir solution containing 15.2% w/v PEG 3350, 2% w/v PEG 8000, 72 mM Tris, pH 8.0, 144 mM magnesium chloride hexahydrate, 20 mM HEPES/sodium hydroxide pH 7.5, 1.6% v/v glycerol, and 8% v/v DMSO, and equilibration against 0.2 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 3.3 A resolution. Purified recombinant detagged mutant truncated enzyme and truncated mutant E137A by sitting drop vapour diffusion, mixing of 0.001 ml of 8 mg/ml protein in 50 mM Tris, pH 8.0, 500 mM NaCl, and 5% glycerol, with 0.001 ml of reservoir solution containing 0.2 M magnesium chloride hexahydrate, 0.1 M Tris, pH 8.5 or pH 6.5, respectively, 25% w/v PEG 3350, and equilibration against 0.1 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.80 and 1.56 A resolution, respectively. Molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D106A
-
variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
D106N
pathogenic variant in the conserved N-terminal domain, eliminates the ability to coordinate the divalent metal ion, abolishes catalytic activity and destabilizes the local protein structure. The protein shows increased alpha-helix content
D30N
pathogenic variant in the conserved N-terminal domain, eliminates the ability to coordinate the divalent metal ion, abolishes catalytic activity and destabilizes the local protein structur. Protein is rapidly degraded
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
R128H
-
enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold
R128Q
pathogenic variant in the conserved N-terminal domain, the protein shows increased alpha-helix content. Complete loss of exopolyphosphatase activity
E112A
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
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
-
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
-
E137A
additional information
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
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (Ppx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+
additional information
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (Ppx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+
additional information
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (mxPpx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+. Deletion of the C-terminal domain in Ppx2 leads to loss of the requirement for K+
additional information
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (mxPpx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+. Deletion of the C-terminal domain in Ppx2 leads to loss of the requirement for K+
additional information
-
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (Ppx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+
-
additional information
-
a fusion protein of the Ppx2 C-terminal domain to Ppx1 (mxPpx1-2C) has significantly reduced exopolyphosphatase activity toward long-chain polyPs (by 90%). Activity toward polyP3 and polyP4 is much less affected while the phosphohydrolase activity toward pppGpp, ATP, and GTP is also decreased (by 30-75%). The fusion protein has increased hydrolytic activity compared to Ppx1 and has aquired the requirement of K+. Deletion of the C-terminal domain in Ppx2 leads to loss of the requirement for K+
-
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 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
-
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
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
incubation of h-prune 1-100 microM for 5 h in the presence of 0.1 M Tris-HCl, pH 7.2, and 0.05 mM EGTA inactivates the enzyme 2-4fold, no inactivation is evident in the presence of 1 mM Mg2+
25 - 40
at pH 6.8, 2 mM MgCl2 and 25 mM KCl, no significant loss of activity is observed after 60 min
45
after preheating at 45°C for 30 and 60 min, 70% and 40% of the PPX2 activity remains
50
after preheating at 50°C, His-tagged PPX2 loses its activity quickly, after incubation for 60 min, no activity remains
60
60
complete inactivation of His-tagged PPX2 within 5 min
60
-
2 min, complete loss of activity, slight protection from heat inactivation, 10%, by 1 mM MnCl2
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 0.05 mM CoSO4 does not increase the enzyme stability independent of the presence of Triton X-100
-
more than 90% loss of activity after freezing in liquid nitrogen and subsequent thawing
-
repeated freezing and thawing destroys activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl buffer, pH 7.6, 10 mM MgCl2, 0.5 mM EDTA, 150 mM NaCl, 20% loss of activity after 2 months
-
-20°C, in 50 mM Tris-HCl buffer, pH 7.5, 5 mM MgCl2, 0.5 mM EDTA, 50 mM NaCl, 0.1% w/v bovine serum albumin, 40% v/v glycerol, exopolyphosphatase I and II, less than 30% loss of activity after 2 months
-
-4°C, enzyme desorbed from heparin-agarose with 1 M KCl and 0.1% Triton X-100, 4 days, no loss of activity
-
-80°C, 300 mM NaCl, 250 mM sucrose, 2 mM dithiothreitiol, several months, no activity loss
-
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
4°C, enzyme obtained by desorption with polyphosphate, 2 h, 30% loss of activity
-
4°C, in absence of detergents, complete loss of activity after 24 h, can be stabilized by 0.1% Triton X-100 and protease inhibitors
-
92°C, in the presence of 0.1% Triton X-100, 5 days, 8% loss of activity of the partially purified exopolyphosphatase preparation after DEAE-Toyopearl chromatography
-
92°C, without 0.1% Triton X-100, 5 days, 66% loss of activity of the partially purified exopolyphosphatase preparation after DEAE-Toyopearl chromatography
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose resin column chromatography or amylose-resin column chromatography
isolation of a recombinant His-tagged protein by affinity chromatography followed by cleavage of the polyhistidine tag
-
isolation of two isoenzymes by cellular fractionation and gel filtration
-
recombinant enzyme PPX1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain Rosetta-Gami B (DE3)pLysS by nickel affinity chromatography
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration, followed by cleavage of the His tag by PreScission protease, and gel filtration
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus by nickel affinity chromatography, dialysis, tag cleavage thriugh thrombin, and again dialysis
-
recombinant ppx2 enzyme is purified by Ni-nitrilotriacetic acid chromatography
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3)
expressed and purified as MBP fusion proteins from Escherichia coli
expressed in Escherichia coli as His-tagged wild type protein and His-tagged variants
-
expression in Escherichia coli
expression in Escherichia coli, overexpression of ppx2 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene ppa, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta-Gami B (DE3)pLysS
-
gene ppx or Msed_0891, quantitative RT-PCR expression analysis, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene ppx, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strains XL10-Gold and BL21-CodonPlus
gene ppx, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains XL10-Gold and BL21-CodonPlus
-
gene ppx1, recombinant overexpression in Saccharomyces cerevisiae strain CRN
overexpression of ppx1 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3), recombinant overexpression in Trypanosoma brucei procyclic 29-13 TetR/T7RNAP cell line
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
transfected into HEK-293 cell. Mutant D30N and D106N protein is rapidly degraded after expression, wild-type and mutant R128Q protein is stable. Lysates from cells expressing mutant G174* show no discernable protein product
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is increased by about 10fold, in low oxygen growth conditions
expression is increased by about 25fold, in low oxygen growth conditions
gene ppx is upregulated upon copper exposure
under nitrogen-limiting conditions, exopolyphosphatase expression is controlled from a sigma54-dependent promoter activated by the response regulator NtrC. Under phosphate limitation, the expression is controlled from a sigma70 promoter, activated by PhoB
expression is increased by about 10fold, in low oxygen growth conditions
expression is increased by about 10fold, in low oxygen growth conditions
-
-
expression is increased by about 25fold, in low oxygen growth conditions
expression is increased by about 25fold, in low oxygen growth conditions
-
-
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Properties of apyrase and inorganic pyrophosphatase in Streptomyces aureofaciens
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brenda
Jungnickel, F.
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Cyberlindnera jadinii, Wolffia arrhiza, Lemna trisulca, Lemna minor, Lemna gibba, Solanum tuberosum, Riccia fluitans
-
brenda
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Inorganic phosphatases and phosphagen kinase in Euglena gracilis
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brenda
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Regulative properties of surface located hydrolases in Candida utilis and in some Lemnaceae
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1981
Cyberlindnera jadinii
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brenda
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brenda
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10996-11001
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Saccharomyces cerevisiae
brenda
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90
7029-7033
1993
Escherichia coli
brenda
Kulakovskaya, T.V.; Andreeva, N.A.; Kualev, I.S.
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62
1051-1052
1997
Saccharomyces cerevisiae
brenda
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The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase
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274
236-241
2000
Escherichia coli
brenda
Lorenz, B.; Batel, R.; Bachinski, N.; Mueller, W.E.G.; Schroeder, H.C.
Purification and characterization of two exopolyphosphatases from the marine sponge Tethya lyncurium
Biochim. Biophys. Acta
1245
17-28
1995
Tethya aurantium
brenda
Guranowski, A.; Starzynska, E.; Barnes, L.D.; Robinson, A.K.; Liu, S.
Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1380
232-238
1998
Saccharomyces cerevisiae
brenda
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Partial purification and characterization of nuclear exopolyphosphatase from Saccharomyces cerevisiae strain with inactivated PPX1 gene encoding a major yeast exopolyphosphatase
Biochemistry
69
270-274
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38698), Saccharomyces cerevisiae CRX
brenda
Andreeva, N.A.; Kulakovskaya, T.V.; Kulaev, I.S.
Purification and properties of exopolyphosphatase from the cytosol of Saccharomyces cerevisiae not encoded by the PPX1 gene
Biochemistry
69
387-393
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
brenda
Lichko, L.; Kulakovskaya, T.; Kulaev, I.
Effect of PPX1 inactivation on exopolyphosphatases of different cell compartments of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1599
102-105
2002
Saccharomyces cerevisiae
brenda
Lichko, L.; Kulakovskaya, T.; Kulaev, I.
Inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1 in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1674
98-102
2004
Saccharomyces cerevisiae
brenda
Rodrigues, C.O.; Ruiz, F.A.; Vieira, M.; Hill, J.E.; Docampo, R.
An acidocalcisomal exopolyphosphatase from Leishmania major with high affinity for short chain polyphosphate
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277
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Leishmania major
brenda
Proudfoot, M.; Kuznetsova, E.; Brown, G.; Rao, N.N.; Kitagawa, M.; Mori, H.; Savchenko, A.; Yakunin, A.F.
General Enzymatic Screens Identify Three New Nucleotidases in Escherichia coli. Biochemical Characterization of SurE, YfbR, and Yjjg
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279
54687-54694
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Escherichia coli (P0A840)
brenda
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Two exopolyphosphatases of Microlunatus phosphovorus, a polyphosphate-accumulating eubacterium from activated sludge
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37
799-803
2002
Microlunatus phosphovorus
-
brenda
Zago, A.; Chugani, S.; Chakrabarty, A.M.
Cloning and characterization of polyphosphate kinase and exopolyphosphatase genes from Pseudomonas aeruginosa 8830
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65
2065-2071
1999
Pseudomonas aeruginosa (Q9S605), Pseudomonas aeruginosa, Pseudomonas aeruginosa 8830 (Q9S605), Pseudomonas aeruginosa 8830
brenda
Kulakovskaya, T.V.; Andreeva, N.A.; Trilisenko, L.V.; Suetin, S.V.; Vagabov, V.M.; Kulaev, I.S.
Accumulation of polyphosphates and expression of high molecular weight exopolyphosphatase in the yeast Saccharomyces cerevisiae
Biochemistry
70
980-985
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
brenda
Andreeva, N.A.; Kulakovskaya, T.V.; Kulaev, I.S.
High Molecular Mass Exopolyphosphatase from the Cytosol of the Yeast Saccharomyces cerevisiae Is Encoded by the PPN1 Gene
Biochemistry (Moscow)
71
975-977
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
brenda
Lichko, L.; Kulakovskaya, T.; Pestov, N.; Kulaev, I.
Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes
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brenda
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Saccharomyces cerevisiae
brenda
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359
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The effect of inactivation of the exo- and endopolyphosphatase genes PPX1 and PPN1 on the level of different polyphosphates in the yeast Saccharomyces cerevisiae
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75
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2006
Saccharomyces cerevisiae
-
brenda
Lichko, L.P.; Kulakovskaya, T.V.; Pestov, N.A.; Kulaev, I.S.
Inactivation of the PPN1 gene exerts different effects on the metabolism of inorganic polyphosphates in the cytosol and the vacuoles of the yeast Saccharomyces cerevisiae
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75
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2006
Saccharomyces cerevisiae
-
brenda
Kulakovskaya, T.V.; Andreeva, N.A.; Trilisenko, L.V.; Vagabov, V.M.; Kulaev, I.S.
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39
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Saccharomyces cerevisiae
-
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Structure
14
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2006
Escherichia coli
brenda
Cardona, S.T.; Chavez, F.P.; Jerez, C.A.
The exopolyphosphatase gene from Sulfolobus solfataricus: characterization of the first gene found to be involved in polyphosphate metabolism in archaea
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68
4812-4819
2002
Saccharolobus solfataricus (Q97YV9), Saccharolobus solfataricus
brenda
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Inorganic polyphosphates and exopolyphosphatases in different cell compartments of Saccharomyces cerevisiae
Biochemistry (Moscow)
71
1171-1175
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae CRY
brenda
Andreeva, N.A.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Kulaev, I.S.
Polyphosphates and exopolyphosphatases in cytosol and mitochondria of Saccharomyces cerevisiae during growth on glucose or ethanol under phosphate surplus
Biochemistry (Moscow)
73
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Saccharomyces cerevisiae
brenda
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37
1103-1107
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Rhipicephalus microplus
brenda
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282
32501-32510
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Trypanosoma cruzi (Q6Y656), Trypanosoma cruzi
brenda
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Kinetic and mutational analyses of the major cytosolic exopolyphosphatase from Saccharomyces cerevisiae
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282
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Saccharomyces cerevisiae, Saccharomyces cerevisiae AH22
brenda
Ugochukwu, E.; Lovering, A.L.; Mather, O.C.; Young, T.W.; White, S.A.
The crystal structure of the cytosolic exopolyphosphatase from Saccharomyces cerevisiae reveals the basis for substrate specificity
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371
1007-1021
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Saccharomyces cerevisiae
brenda
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Inorganic polyphosphate and exopolyphosphatase in the nuclei of Saccharomyces cerevisiae: dependence on the growth phase and inactivation of the PPX1 and PPN1 genes
Yeast
23
735-740
2006
Saccharomyces cerevisiae
brenda
Lichko, L.P.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Kulaev, I.S.
Inactivation of PPX1 and PPN1 genes encoding exopolyphosphatases of Saccharomyces cerevisiae does not prevent utilization of polyphosphates as phosphate reserve
Biochemistry (Moscow)
73
985-989
2008
Saccharomyces cerevisiae
brenda
Tammenkoski, M.; Koivula, K.; Cusanelli, E.; Zollo, M.; Steegborn, C.; Baykov, A.A.; Lahti, R.
Human metastasis regulator protein H-prune is a short-chain exopolyphosphatase
Biochemistry
47
9707-9713
2008
Homo sapiens
brenda
Campos, E.; Facanha, A.R.; Costa, E.P.; da Silva Vaz, I.; Masuda, A.; Logullo, C.
Exopolyphosphatases in nuclear and mitochondrial fractions during embryogenesis of the hard tick Rhipicephalus (Boophilus) microplus
Comp. Biochem. Physiol. B
151
311-316
2008
Rhipicephalus microplus
brenda
Lindner, S.N.; Knebel, S:; Wesseling,H.; Schoberth, S.M.; Wendisch, V.F.
Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum[down-pointing small open triangle]
Appl. Environ. Microbiol.
75
3161-3170
2009
Corynebacterium glutamicum (Q8NT99), Corynebacterium glutamicum (Q8NRR8), Corynebacterium glutamicum
brenda
Varela, C.; Mauriaca, C.; Paradela, A.; Albar, J.P.; Jerez, C.A.; Chavez, F.P.
New structural and functional defects in polyphosphate deficient bacteria: A cellular and proteomic study
BMC Microbiol.
10
7-7
2010
Pseudomonas sp.
brenda
Luginbuehl, E.; Kunz, S.; Wentzinger, L.; Freimoser, F.; Seebeck, T.
The exopolyphosphatase TbrPPX1 of Trypanosoma brucei
BMC Microbiol.
11
4-4
2011
Trypanosoma brucei (Q7Z032), Trypanosoma brucei, Trypanosoma brucei 427 (Q7Z032)
brenda
Zhang, Q.; Li, Y.; Tang, C.M.
The role of the exopolyphosphatase PPX in avoidance by Neisseria meningitidis of complement-mediated killing
J. Biol. Chem.
285
34259-34268
2010
Neisseria meningitidis
brenda
Campos, E.; Facanha, A.R.; Costa, E.P.; Fraga, A.; Moraes, J.; da Silva Vaz, I.; Masuda, A.; Logullo, C.
A mitochondrial membrane exopolyphosphatase is modulated by, and plays a role in, the energy metabolism of hard tick Rhipicephalus (Boophilus) microplus embryos
Int. J. Mol. Sci.
12
3525-3535
2011
Rhipicephalus microplus
brenda
Thayil, S.M.; Morrison, N.; Schechter, N.; Rubin, H.; Karakousis, P.C.
The role of the novel exopolyphosphatase MT0516 in Mycobacterium tuberculosis drug tolerance and persistence
PLoS ONE
6
e28076
2011
Mycobacterium tuberculosis (P9WHV4), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (P9WHV4)
brenda
Remonsellez, F.; Orell, A.; Jerez, C.A.
Copper tolerance of the thermoacidophilic archaeon Sulfolobus metallicus: possible role of polyphosphate metabolism
Microbiology
152
59-66
2006
Sulfuracidifex metallicus, Sulfuracidifex metallicus DSM 6482
brenda
Andreeva, N.; Trilisenko, L.; Kulakovskaya, T.; Dumina, M.; Eldarov, M.
Purification and properties of recombinant exopolyphosphatase PPN1 and effects of its overexpression on polyphosphate in Saccharomyces cerevisiae
J. Biosci. Bioeng.
119
52-56
2015
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
brenda
Albi, T.; Serrano, A.
Two exopolyphosphatases with distinct molecular architectures and substrate specificities from the thermophilic green-sulfur bacterium Chlorobium tepidum TLS
Microbiology
160
2067-2078
2014
Chlorobaculum tepidum (Q8KG69), Chlorobaculum tepidum (Q8KBS0), Chlorobaculum tepidum DSM 12025 (Q8KG69), Chlorobaculum tepidum DSM 12025 (Q8KBS0)
brenda
Gallarato, L.A.; Sanchez, D.G.; Olvera, L.; Primo, E.D.; Garrido, M.N.; Beassoni, P.R.; Morett, E.; Lisa, A.T.
Exopolyphosphatase of Pseudomonas aeruginosa is essential for the production of virulence factors, and its expression is controlled by NtrC and PhoB acting at two interspaced promoters
Microbiology
160
406-417
2014
Pseudomonas aeruginosa (Q9ZN70), Pseudomonas aeruginosa
brenda
Andreeva, N.; Trilisenko, L.; Eldarov, M.; Kulakovskaya, T.
Polyphosphatase PPN1 of Saccharomyces cerevisiae: switching of exopolyphosphatase and endopolyphosphatase activities
PLoS ONE
10
e0119594
2015
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
brenda
Choi, M.Y.; Wang, Y.; Wong, L.L.; Lu, B.T.; Chen, W.Y.; Huang, J.D.; Tanner, J.A.; Watt, R.M.
The two PPX-GppA homologues from Mycobacterium tuberculosis have distinct biochemical activities
PLoS ONE
7
e42561
2012
Mycobacterium tuberculosis (P9WHV5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHV5)
brenda
Malde, A.; Gangaiah, D.; Chandrashekhar, K.; Pina-Mimbela, R.; Torrelles, J.B.; Rajashekara, G.
Functional characterization of exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) of Campylobacter jejuni
Virulence
5
521-533
2014
Campylobacter jejuni (A0A0H3PES2), Campylobacter jejuni (A0A0H3PAT6), Campylobacter jejuni 81-176 (A0A0H3PES2), Campylobacter jejuni 81-176 (A0A0H3PAT6)
brenda
Zhang, A.; Guo, E.; Qian, L.; Tang, N.Y.; Watt, R.M.; Bartlam, M.
Purification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis
Acta Crystallogr. Sect. F
72
172-178
2016
Zymomonas mobilis (A0A542W0V0), Zymomonas mobilis, Zymomonas mobilis NCIMB 11163 (A0A542W0V0)
brenda
Boetsch, C.; Aguayo-Villegas, D.R.; Gonzalez-Nilo, F.D.; Lisa, A.T.; Beassoni, P.R.
Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
Arch. Biochem. Biophys.
606
64-72
2016
Escherichia coli (P0AFL6), Escherichia coli
brenda
Rivero, M.; Torres-Paris, C.; Munoz, R.; Cabrera, R.; Navarro, C.A.; Jerez, C.A.
Inorganic polyphosphate, exopolyphosphatase, and Pho84-like transporters may be involved in copper resistance in Metallosphaera sedula DSM 5348T
Archaea
2018
5251061
2018
Metallosphaera sedula (A4YFE8), Metallosphaera sedula, Metallosphaera sedula DSM 5348 (A4YFE8), Metallosphaera sedula ATCC 51363 (A4YFE8), Metallosphaera sedula JCM 9185 (A4YFE8), Metallosphaera sedula NBRC 15509 (A4YFE8), Metallosphaera sedula TH2 (A4YFE8)
brenda
Andreeva, N.; Ledova, L.; Ryazanova, L.; Tomashevsky, A.; Kulakovskaya, T.; Eldarov, M.
Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae Comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases
Biochimie
163
101-107
2019
Saccharomyces cerevisiae (P38698), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38698)
brenda
Cordeiro, C.D.; Ahmed, M.A.; Windle, B.; Docampo, R.
NUDIX hydrolases with inorganic polyphosphate exo- and endopolyphosphatase activities in the glycosome, cytosol and nucleus of Trypanosoma brucei
Biosci. Rep.
39
BSR20190894
2019
Trypanosoma brucei brucei (Q57Z14), Trypanosoma brucei brucei (Q583R7), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q57Z14), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q583R7)
brenda
Beassoni, P.R.; Gallarato, L.A.; Boetsch, C.; Garrido, M.N.; Lisa, A.T.
Pseudomonas aeruginosa exopolyphosphatase is also a polyphosphate ADP phosphotransferase
Enzyme Res.
2015
404607
2015
Pseudomonas aeruginosa
brenda
Cruz, C.S.; Costa, E.P.; Machado, J.A.; Silva, J.N.; Romeiro, N.C.; Moraes, J.; Silva, J.R.; Fonseca, R.N.; Vaz, I.S.; Logullo, C.; Campos, E.
A soluble inorganic pyrophosphatase from the cattle tick Rhipicephalus microplus capable of hydrolysing polyphosphates
Insect Mol. Biol.
27
260-267
2018
Rhipicephalus microplus
brenda
Corrales, D.; Alcantara, C.; Zuniga, M.; Monedero, V.
Ppx1 putative exopolyphosphatase is essential for polyphosphate accumulation in Lacticaseibacillus paracasei
Appl. Environ. Microbiol.
90
e0229023
2024
Lacticaseibacillus paracasei
brenda
Hiyoshi, T.; Oyanagi, K.; Niki, T.; Fujiwara, S.; Sato, N.
Requirement of the exopolyphosphatase gene for cellular acclimation to phosphorus starvation in a cyanobacterium, Synechocystis sp. PCC 6803
Biochem. Biophys. Res. Commun.
540
16-21
2021
Synechocystis sp. PCC 6803 (P74663)
brenda
Harita, D.; Kanie, K.; Kimura, Y.
Enzymatic properties of Myxococcus xanthus exopolyphosphatases mxPpx1 and mxPpx2
Biochim. Biophys. Acta Proteins Proteom.
1869
140660
2021
Myxococcus xanthus (Q1D0C7), Myxococcus xanthus (Q1CYS6), Myxococcus xanthus DK1622 (Q1D0C7), Myxococcus xanthus DK1622 (Q1CYS6)
brenda
Nistala, H.; Dronzek, J.; Gonzaga-Jauregui, C.; Chim, S.M.; Rajamani, S.; Nuwayhid, S.; Delgado, D.; Burke, E.; Karaca, E.; Franklin, M.C.; Sarangapani, P.; Podgorski, M.; Tang, Y.; Dominguez, M.G.; Withers, M.; Deckelbaum, R.A.; Scheonherr, C.J.; Gahl, W.A.; Malicdan, M.C.; Zambrowicz, B.; Gale, N.W.; , G.
NMIHBA results from hypomorphic PRUNE1 variants that lack short-chain exopolyphosphatase activity
Hum. Mol. Genet.
29
3516-3531
2021
Homo sapiens (Q86TP1)
brenda
Lu, Z.; Hu, Y.; Wang, J.; Zhang, B.; Zhang, Y.; Cui, Z.; Zhang, L.; Zhang, A.
Structure of the exopolyphosphatase (PPX) from Zymomonas mobilis reveals a two-magnesium-ions PPX
Int. J. Biol. Macromol.
262
129796
2024
Zymomonas mobilis subsp. mobilis (Q5NPM3), Zymomonas mobilis subsp. mobilis ATCC 31821 (Q5NPM3)
brenda
Zhang, A.; Lu, Z.; Xu, Y.; Qi, T.; Li, W.; Zhang, L.; Cui, Z.
The structure of exopolyphosphatase (PPX) from Porphyromonas gingivalis in complex with substrate analogs and magnesium ions reveals the basis for polyphosphate processivity
J. Struct. Biol.
213
107767
2021
Porphyromonas gingivalis (B2RHQ2), Porphyromonas gingivalis DSM 20709 (B2RHQ2)
brenda
Tiwari, P.; Gosain, T.P.; Chugh, S.; Singh, M.; Sankhe, G.D.; Arora, G.; Kidwai, S.; Agarwal, S.; Saini, D.K.; Singh, R.
Exopolyphosphatases PPX1 and PPX2 from Mycobacterium tuberculosis regulate dormancy response and pathogenesis
Microb. Pathog.
173
105885
2022
Mycobacterium tuberculosis (P9WHV5), Mycobacterium tuberculosis (P96374), Mycobacterium tuberculosis H37Rv (P9WHV5), Mycobacterium tuberculosis H37Rv (P96374)
brenda
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