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Literature summary extracted from

  • 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 (2008), Biochemistry, 47, 9707-9713.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.11 expressed in Escherichia coli as His-tagged wild type protein and His-tagged variants Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.11 D106A variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart Homo sapiens
3.6.1.11 D179A variant is inactive Homo sapiens
3.6.1.11 D28A variant is inactive Homo sapiens
3.6.1.11 H107N variant displays reduced activity with a turnover value of 4.4% compared to the wild type counterpart, Km value increases 7fold Homo sapiens
3.6.1.11 H108N variant displays reduced activity with a turnover value of 32% compared to the wild type counterpart Homo sapiens
3.6.1.11 N24H variant is inactive Homo sapiens
3.6.1.11 R128H enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold Homo sapiens
3.6.1.11 R348A variant is inactive Homo sapiens

General Stability

EC Number General Stability Organism
3.6.1.11 Mg2+ stabilizes h-prune against inactivation during storage Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.11 (phosphate)25
-
Homo sapiens
3.6.1.11 (phosphate)45
-
Homo sapiens
3.6.1.11 (phosphate)65
-
Homo sapiens
3.6.1.11 diphosphate potential physiological regulator Homo sapiens
3.6.1.11 dipyridamole known inhibitor of phosphodiesterase, no effect on the triphosphate hydrolyzing activity of h-prune Homo sapiens
3.6.1.11 long-chain polyphosphate potential physiological regulator, inhibits h-prune-catalyzed hydrolysis of triphosphate Homo sapiens
3.6.1.11 additional information nucleoside triphosphates, diadenosine hexaphosphate, cAMP and dipyridamole do not affect the activity Homo sapiens
3.6.1.11 nm23-H1 metastasis suppressor protein, the exopolyphosphatase activity is suppressed Homo sapiens
3.6.1.11 ZnCl2
-
Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.11 0.0007
-
(phosphate)65 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0012
-
(phosphate)3 D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0022
-
(phosphate)3 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0022
-
(phosphate)45 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0026
-
(phosphate)3 H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0066
-
(phosphate)3 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.0069
-
(phosphate)25 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.015
-
(phosphate)3 H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.019
-
(phosphate)4 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.028
-
adenosine 5'-tetraphosphate 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.037
-
adenosine 5'-tetraphosphate 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.041
-
(phosphate)4 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.041
-
guanosine 5'-tetraphosphate 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.046
-
(phosphate)3 R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.099
-
guanosine 5'-tetraphosphate 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.11 Co2+ reaction requires a divalent metal cofactor Homo sapiens
3.6.1.11 Mg2+ reaction requires a divalent metal cofactor, bound substrate enhances enzyme affinity for the metal ion Homo sapiens
3.6.1.11 Mn2+ reaction requires a divalent metal cofactor, Mn2+ confers 50% activity compared to Mg2+ in P3 and P4 hydrolysis Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.11 50000
-
estimated from the amino acid composition Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.11 (phosphate)n + H2O Homo sapiens h-prune efficiently hydrolyzes short-chain polyphosphates (phosphate)n-1 + phosphate
-
?
3.6.1.11 additional information Homo sapiens 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.11 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.11 by metal chelate chromatography Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.11 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 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.11 (phosphate)25 + H2O
-
Homo sapiens (phosphate)24 + phosphate
-
?
3.6.1.11 (phosphate)4 + H2O
-
Homo sapiens (phosphate)3 + phosphate
-
?
3.6.1.11 (phosphate)45 + H2O
-
Homo sapiens (phosphate)44 + phosphate
-
?
3.6.1.11 (phosphate)65 + H2O
-
Homo sapiens (phosphate)64 + phosphate
-
?
3.6.1.11 (phosphate)n + H2O h-prune efficiently hydrolyzes short-chain polyphosphates Homo sapiens (phosphate)n-1 + phosphate
-
?
3.6.1.11 adenosine 5'-tetraphosphate + H2O
-
Homo sapiens ATP + phosphate
-
?
3.6.1.11 guanosine 5'-tetraphosphate + H2O
-
Homo sapiens GTP + phosphate
-
?
3.6.1.11 additional information h-prune is the missing exopolyphosphatase in animals and support the hypothesis that the metastatic effects of h-prune are modulated by inorganic polyphosphates, which are increasingly recognized as critical regulators in cells Homo sapiens ?
-
?
3.6.1.11 triphosphate + H2O
-
Homo sapiens diphosphate + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.11 exopolyphosphatase
-
Homo sapiens
3.6.1.11 h-prune
-
Homo sapiens
3.6.1.11 PPX
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.11 25
-
assay at Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.11
-
-
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+ Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.11 0.03
-
(phosphate)65 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.16
-
(phosphate)25 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.22
-
(phosphate)45 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 0.57
-
(phosphate)3 H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 3.4
-
(phosphate)4 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 4.2
-
(phosphate)3 H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 4.6
-
(phosphate)3 D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 7.1
-
(phosphate)4 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 13
-
(phosphate)3 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 19
-
(phosphate)3 R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 24
-
guanosine 5'-tetraphosphate 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 27
-
guanosine 5'-tetraphosphate 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 31
-
adenosine 5'-tetraphosphate 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 35
-
(phosphate)3 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens
3.6.1.11 39
-
adenosine 5'-tetraphosphate 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.6.1.11 additional information
-
2 mM Mg2+, 60 microM (phosphate)25, 10 mM triphosphate, IC50 is above 0.01 mM Homo sapiens nm23-H1
3.6.1.11 0.0019
-
2 mM Mg2+, 10 mM triphosphate Homo sapiens nm23-H1
3.6.1.11 0.0072
-
2 mM Mg2+, 10 mM triphosphate Homo sapiens nm23-H1
3.6.1.11 0.032
-
2 mM Mg2+, hydrolysis of triphospate is inhibited Homo sapiens ZnCl2
3.6.1.11 0.055
-
2 mM Mg2+, 10 mM triphosphate Homo sapiens (phosphate)45
3.6.1.11 0.064
-
c2 mM Mg2+, 10 mM triphosphate Homo sapiens (phosphate)65
3.6.1.11 0.105
-
c2 mM Mg2+, 100 mM triphosphate Homo sapiens (phosphate)65
3.6.1.11 0.12
-
2 mM Mg2+, 100 mM triphosphate Homo sapiens (phosphate)45
3.6.1.11 0.163
-
2 mM Mg2+, 10 mM triphosphate Homo sapiens (phosphate)25
3.6.1.11 0.33
-
2 mM Mg2+, 100 mM triphosphate Homo sapiens (phosphate)25
3.6.1.11 1.2
-
2 mM Mg2+, 10 mM triphosphate Homo sapiens diphosphate
3.6.1.11 5.7
-
2 mM Mg2+, 100 mM triphosphate Homo sapiens diphosphate