Information on EC 3.6.1.10 - endopolyphosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.6.1.10
-
RECOMMENDED NAME
GeneOntology No.
endopolyphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
polyphosphate + n H2O = (n+1) oligophosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
polyphosphate polyphosphohydrolase
The product contains 4 or 5 phosphate residues.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-86-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Chlamydomonas sp.
low activity
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
28610
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
Pyrococcus islandicum
low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
polyphosphate + H2O
oligophosphate
show the reaction diagram
polyphosphate 208 + H2O
oligophosphate
show the reaction diagram
-
-
the average polyphosphate chain lengths decrease from about 208 to about 10 phosphate residues
-
?
polyphosphate 208 + H2O
polyphosphate 193 + polyphosphate 15
show the reaction diagram
-
-
-
-
?
polyphosphate700 + H2O
phosphate + triphosphate
show the reaction diagram
progression via intermediate chain length polyphosphates
product analysis
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
0.01-1 mM, activation
Ca2+
-
activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
Ca2+
-
0.01 mM
CaCl2
-
1 mM, 35% inhibition
Citric acid
-
-
diphosphate
-
10 mM, complete inhibition
EDTA
-
10 mM, complete inhibition
phloretin phosphate
-
-
phosphate
-
20 mM, 50% inhibition
ZnCl2
-
1 mM, 35% inhibition
additional information
-
the enzyme is insensitive to 5 mM fluoride
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000185
polyP750
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
phosphate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
purified native Ppn1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 3.4
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-
5.7
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hydrolysis of polymetaphosphate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
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low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
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activity is greater in mycorrhizal roots of Allium cepa than in non-mycorrhizal roots
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
gel filtration
34500
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
35000
-
2 * 35000, SDS-PAGE
80000
-
gel filtration
142000
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 35000, SDS-PAGE
tetramer
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
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loss of activity above
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Toyopearl 650M column chromatography, heparin agarose column chromatography, and Mono Q column chromatography
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native enzyme from exopolyphosphatase-deficient mutant strain CRX by heparin affinity and phosphocellulose chromatography, 3820fold to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
gene ppn1, DNA and amino acid sequence determination and analysis, expression of wild-type pre-Ppn1 and mutants in Escherichia coli and in HEK-293 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
the overexpression of the processed form of the enzyme should provide a unique and powerful reagent to analyze inorganic polyphosphate when the chain termini are unavailable to the actions of polyPase and polyP kinase
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