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Enzyme Nomenclature
Information on EC 3.6.1.10 - endopolyphosphatase
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
3.6.1.10
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RECOMMENDED NAME
GeneOntology No.
endopolyphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
polyphosphate + n H2O = (n+1) oligophosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate polyphosphohydrolase
The product contains 4 or 5 phosphate residues.
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CAS REGISTRY NUMBER
COMMENTARY
9024-86-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional exo- and endopolyphosphatase, EC 3.6.1.11 and EC 3.6.1.10
SwissProt
strain CRX, CRY, CRN, and CNX derived from strain W303-1A
SwissProt
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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
polyphosphate 208 + H2O
oligophosphate
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the average polyphosphate chain lengths decrease from about 208 to about 10 phosphate residues
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?
polyphosphate 208 + H2O
polyphosphate 193 + polyphosphate 15
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-
?
polyphosphate700 + H2O
phosphate + triphosphate
progression via intermediate chain length polyphosphates
product analysis
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?
polyphosphate + H2O
oligophosphate
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polymetaphosphate
break down stops when the scission products are tetraphosphate or pentaphosphate
?
polyphosphate + H2O
oligophosphate
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distributive action on polyP750 produces shorter chains to a limit of about polyP60 as well as the more abundant release of polyP3, limit digestion product is polyP3
?
additional information
?
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inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
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additional information
?
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null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
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additional information
?
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the pathway of particular polyphosphates in yeast is different with endo- and exopolyphosphatase playing critical roles
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additional information
?
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enzyme is a bifunctional exo- and endopolyphosphatase, activities of ECs 3.6.1.11 and 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenyl phosphate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
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inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
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additional information
?
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Q04119
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
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additional information
?
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the pathway of particular polyphosphates in yeast is different with endo- and exopolyphosphatase playing critical roles
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
additional information
Mg2+
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity
additional information
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addition of 3 mM Mg2+ and 3 mM Co2+ has no effect on the cytosol endopolyphosphatase activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
additional information
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the enzyme is insensitive to 5 mM fluoride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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activity is greater in mycorrhizal roots of Allium cepa than in non-mycorrhizal roots
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34500
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
both the C-terminus and the N-terminus of Ppn1 are cleaved during enzyme activation
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
additional information
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
additional information
construction of Ppn1 mutants, overview
additional information
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inactivation of gene ppn1 encoding the endopolyphosphatase PPN1 togehther with inactivation of exopolyphosphatase PPX1 leads to a two-fold increase in high-molecular weight alkali-soluble polyphosphates in yeast cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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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LINKS TO OTHER DATABASES (specific for EC-Number 3.6.1.10)
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