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Information on EC 3.6.1.11 - exopolyphosphatase and Organism(s) Homo sapiens
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3.6.1.11 exopolyphosphataseSpecify your search results
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
exopolyphosphatase, polyphosphate phosphatase, polyphosphate phosphohydrolase, exopolypase, rv0496, exopoly(p)ase, pappx, exopolyphosphatase 1, lmppx, high molecular weight exopolyphosphatase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid phosphoanhydride phosphohydrolase
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exopoly(P)ase
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ExopolyPase
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Gra-Pase
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metaphosphatase
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phosphatase, exopoly-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(phosphate)n + H2O
(phosphate)n-1 + phosphate
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h-prune efficiently hydrolyzes short-chain polyphosphates
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additional information
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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
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(phosphate)n + H2O
(phosphate)n-1 + phosphate
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h-prune efficiently hydrolyzes short-chain polyphosphates
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?
additional information
?
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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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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reaction requires a divalent metal cofactor, bound substrate enhances enzyme affinity for the metal ion
Mn2+
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reaction requires a divalent metal cofactor, Mn2+ confers 50% activity compared to Mg2+ in P3 and P4 hydrolysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dipyridamole
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known inhibitor of phosphodiesterase, no effect on the triphosphate hydrolyzing activity of h-prune
long-chain polyphosphate
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potential physiological regulator, inhibits h-prune-catalyzed hydrolysis of triphosphate
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nm23-H1
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metastasis suppressor protein, the exopolyphosphatase activity is suppressed
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additional information
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nucleoside triphosphates, diadenosine hexaphosphate, cAMP and dipyridamole do not affect the activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0069
(phosphate)25
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.0022
(phosphate)45
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.0007
(phosphate)65
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.0012
(phosphate)3
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D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0022
(phosphate)3
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0026
(phosphate)3
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H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.0066
(phosphate)3
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.015
(phosphate)3
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H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.046
(phosphate)3
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R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.019
(phosphate)4
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.041
(phosphate)4
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.028
adenosine 5'-tetraphosphate
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.037
adenosine 5'-tetraphosphate
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.041
guanosine 5'-tetraphosphate
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
0.099
guanosine 5'-tetraphosphate
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
(phosphate)25
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.22
(phosphate)45
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.03
(phosphate)65
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
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0.57
(phosphate)3
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H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
4.2
(phosphate)3
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H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
4.6
(phosphate)3
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D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
19
(phosphate)3
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R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
31
adenosine 5'-tetraphosphate
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
39
adenosine 5'-tetraphosphate
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
24
guanosine 5'-tetraphosphate
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2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
27
guanosine 5'-tetraphosphate
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2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
nm23-H1
Homo sapiens
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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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D106A
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variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
H107N
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variant displays reduced activity with a turnover value of 4.4% compared to the wild type counterpart, Km value increases 7fold
H108N
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variant displays reduced activity with a turnover value of 32% compared to the wild type counterpart
R128H
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enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
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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+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tagged wild type protein and His-tagged variants
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 3.6.1.11)
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