Information on EC 3.6.1.11 - exopolyphosphatase

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

EC NUMBER
COMMENTARY
3.6.1.11
-
RECOMMENDED NAME
GeneOntology No.
exopolyphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
show the reaction diagram
the interaction of the enzyme with polyphosphate is independent on cation concentration, binding is not driven by entropy from release of polyelectrolyte condensed cations
-
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
show the reaction diagram
hydrolyzes poly-phosphates with an average chain length of 208 to 15 phosphate residues
-
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
show the reaction diagram
hydrolyzes poly-phosphates with an average chain length of 208 to 15 phosphate residues
Saccharomyces cerevisiae VKM Y-1173
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
P0A840
-
phosphorous acid anhydride hydrolysis
-
-
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
P0A840
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-, Q8NRR8, Q8NT99
;
phosphorous acid anhydride hydrolysis
Saccharomyces cerevisiae VKM Y-1173
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
polyphosphate phosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40 kD exopolyphosphatase
-
-
40 kD exopolyphosphatase
Saccharomyces cerevisiae VKM Y-1173
-
-
-
40-kDa-exopolyphosphatase
-
-
acid phosphoanhydride phosphohydrolase
-
-
-
-
exopoly(P)ase
-
-
-
-
ExopolyPase
-
-
-
-
exopolyphosphatase
Q8NRR8, Q8NT99
-
exopolyphosphatase
-
-
exopolyphosphatase
-
-
exopolyphosphatase
-
-
exopolyphosphatase
-
-
exopolyphosphatase 1
-
-
exopolyphosphatase 2
-
-
Gra-Pase
-
-
-
-
h-prune
-
-
high molecular mass exopolyphosphatase
-
-
high molecular mass exopolyphosphatase
Saccharomyces cerevisiae VKM Y-1173
-
;
-
high molecular weight exopolyphosphatase
-
-
high molecular weight exopolyphosphatase
Saccharomyces cerevisiae VKM Y-1173
-
-
-
high-molecular exopolyphosphatase
-
-
major cytosolic exopolyphosphatase PPX1
-
-
major cytosolic exopolyphosphatase PPX1
Saccharomyces cerevisiae CRX
-
-
-
membrane-bound exopolyphosphatase
-
-
MT0516
Mycobacterium tuberculosis CDC 1551
P65786
-
-
nuclear exopolyphosphatase
-
-
nuclear exopolyphosphatase
Saccharomyces cerevisiae CRX
-
-
-
phosphatase, exopoly-
-
-
-
-
polyphosphate phosphatase
-
-
polyphosphate phosphohydrolase
-
-
polyphosphate phosphohydrolase
-
-
polyphosphate phosphohydrolase
Saccharomyces cerevisiae VKM Y-1173
-
-
-
polyphosphate-phosphohydrolase
-
-
polyphosphate-phosphohydrolase
-
-
polyphosphate-phosphohydrolase
Saccharomyces cerevisiae VKM Y-1173
-
;
-
Ppn1
Saccharomyces cerevisiae CRY
-
-
-
PPX
Mycobacterium tuberculosis CDC 1551
P65786
-
-
PPX
Pseudomonas aeruginosa 8830
Q9S605
-
-
PPX
Saccharomyces cerevisiae AH22
-
-
-
PPX
Sulfolobus metallicus DSM 6482
-
-
-
PPX
Q6Y656
-
Ppx protein
-
-
PPX1
Saccharomyces cerevisiae CRY
-
-
-
PPX1
Q7Z032
-
PPX1
Trypanosoma brucei 427
Q7Z032
-
-
vacuolar exopolyphosphatase
-
-
metaphosphatase
-
-
-
-
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
Saccharomyces cerevisiae AH22
-
PPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase, PPase
-
CAS REGISTRY NUMBER
COMMENTARY
9024-85-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
-
-
Manually annotated by BRENDA team
strain BL21(DE3)
-
-
Manually annotated by BRENDA team
strain O157:H7
-
-
Manually annotated by BRENDA team
promastigotes
-
-
Manually annotated by BRENDA team
NM-1 strain, two isoenzymes polyphosphatases I and II
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis CDC 1551
-
UniProt
Manually annotated by BRENDA team
strain 8830
SwissProt
Manually annotated by BRENDA team
Pseudomonas aeruginosa 8830
strain 8830
SwissProt
Manually annotated by BRENDA team
i.e. Boophilus microplus
-
-
Manually annotated by BRENDA team
; strains CRY, CRX, CRN and CNX
-
-
Manually annotated by BRENDA team
CRN and CNX strains,genes ppn1, and ppx1
-
-
Manually annotated by BRENDA team
CRN mutant with inactive PPN1 gene, which is deficient in endopolyphosphatase activity
-
-
Manually annotated by BRENDA team
PPX1 mutant
SwissProt
Manually annotated by BRENDA team
PPX1 mutant, two enzymes with different masses and biochemical properties
-
-
Manually annotated by BRENDA team
strain VKM Y-1173
-
-
Manually annotated by BRENDA team
strain VKM Y-1173 (IBPM-366); VKM Y-1173 strain
-
-
Manually annotated by BRENDA team
strains CRY, CRX, CRN and CNX
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH22
strain AH22
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRX
strain CRX
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRY
strain CRY
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae VKM Y-1173
strain VKM Y-1173
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae VKM Y-1173
strain VKM Y-1173 (IBPM-366); VKM Y-1173 strain
-
-
Manually annotated by BRENDA team
Sulfolobus metallicus DSM 6482
-
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q7Z032, -
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
-, P65786
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
Mycobacterium tuberculosis CDC 1551
-
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
Trypanosoma brucei 427
-
PPX1 genetic ablation does not produce a dramatic phenotype
-
physiological function
-
the biochemical activity of PPX is necessary for interactions with the complement
physiological function
-
exopolyphosphatase activity is regulated during mitochondrial respiration and plays a role in adenosine-5-triphosphate synthesis in hard tick embryos
physiological function
-, P65786
exopolyphosphatase is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
physiological function
Mycobacterium tuberculosis CDC 1551
-
exopolyphosphatase is required for long-term survival of Mycobacterium tuberculosis in necrotic lung lesion
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(phosphate)15 + H2O
(phosphate)14 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)25 + H2O
(phosphate)24 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)4 + H2O
(phosphate)3 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)45 + H2O
(phosphate)44 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)65 + H2O
(phosphate)64 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)65 + H2O
(phosphate)64 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-, P65786
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
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
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-, Q8NRR8, Q8NT99
degradation of polyphosphate
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
h-prune efficiently hydrolyzes short-chain polyphosphates
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
regulatory enzyme in polyphosphate metabolism
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae AH22
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
Mycobacterium tuberculosis CDC 1551
P65786
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRY
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
P38698, -
-
-
-
-
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
ir
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
P0A840
-
-
-
-
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
P38698, -
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Q9S605
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Q7Z032, -
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
n = 500
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
the activity with polyP15 is 85% of that with polyP208, the activity with polyP9 is 24% of that with polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
poly P9-10, polyP33-36
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
n = 10, 25, 50, 100, 250 or 500. n = 250 is the preferred substrate
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
polyP15, polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
n = 40, 72, 180 or 290, highest reaction rate, when n is 40
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
phosphate starvation induces the formation of the enzyme
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
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
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
enzyme is derepressed under phosphate starvation conditions
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
no acyivity if n = 200
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
polyphosphatase I shows optimal activity when n is 25 phosphate residues, polyphosphatases II prefers substrates with 9 residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
chain length of 10-200 phosphate residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Q97YV9, -
n = 500 - 600
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Pseudomonas aeruginosa 8830
Q9S605
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Sulfolobus metallicus DSM 6482
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Trypanosoma brucei 427
Q7Z032
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae VKM Y-1173
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae VKM Y-1173
-
chain length of 10-200 phosphate residues
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Escherichia coli CA10
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRX
-
-
-
-
-
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
P0A840
-
-
-
-
3'-CMP + H2O
cytosine + phosphate
show the reaction diagram
P0A840
-
-
-
-
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
P0A840
-
-
-
-
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
P0A840
-
-
-
-
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
P0A840
-
-
-
-
adenosine 5'-pentaphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
7.3% of the activity with polyP208
-
-
?
guanosine 5'-tetraphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
guanosine 5'-tetraphosphate + H2O
?
show the reaction diagram
Q6Y656, -
-
-
-
?
guanosine 5'-tetraphosphate + H2O
GTP + phosphate
show the reaction diagram
-
-
-
-
?
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
show the reaction diagram
-
-
-
-
?
guanosine-5'-tetraphosphate + H2O
GTP + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
P0A840
-
-
-
-
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
show the reaction diagram
Q7Z032, -
-
-
-
?
pentasodium triphosphate + H2O
pentasodium diphosphate + phosphate
show the reaction diagram
Trypanosoma brucei 427
Q7Z032
-
-
-
?
polyphosphate + H2O
?
show the reaction diagram
-
chain length of more than 45 phosphate residues
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
show the reaction diagram
P38698, -
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
-
-
-
-
?
polyphosphate 15 + H2O
polyphosphate 14 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRX
-
-
-
-
?
polyphosphate 188 + H2O
polyphosphate 187 + phosphate
show the reaction diagram
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
show the reaction diagram
P38698, -
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
show the reaction diagram
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
show the reaction diagram
Saccharomyces cerevisiae VKM Y-1173
-
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRX
-
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
show the reaction diagram
P38698, -
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
-
-
-
-
?
polyphosphate 3 + H2O
polyphosphate 2 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRX
-
-
-
-
?
polyphosphate 75 + H2O
polyphosphate 74 + phosphate
show the reaction diagram
-
-
-
-
?
sodium phosphate glass type 15 + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
tetraphosphate + H2O
triphosphate + phosphate
show the reaction diagram
-, Q8NRR8, Q8NT99
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-, Q8NRR8, Q8NT99
-
-
-
?
triphosphate + H2O
?
show the reaction diagram
Q6Y656, -
-
-
-
?
tripolyphosphate + H2O
phosphate + ?
show the reaction diagram
-
-
-
-
?
tripolyphosphate + H2O
phosphate + ?
show the reaction diagram
-
7.3% of the activity with polyP208
-
-
?
inosine tetraphosphate + H2O
ITP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
-
-
-
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
-
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
-
additional information
?
-
Q6Y656, -
polyphosphates play a role in the parasite's osmoregulation, overview
-
-
-
additional information
?
-
Q6Y656, -
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
-
-
-
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
-
-
-
additional information
?
-
-
PPN1 splitting long polyphosphate chains to shorter ones, PPX1 splitting off phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
-, Q8NRR8, Q8NT99
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
-
-
-
additional information
?
-
Q7Z032, -
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
-
-
-
additional information
?
-
-, P65786
the enzyme does not cleave ppGpp
-
-
-
additional information
?
-
Trypanosoma brucei 427
Q7Z032
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
-
-
-
additional information
?
-
Mycobacterium tuberculosis CDC 1551
P65786
the enzyme does not cleave ppGpp
-
-
-
additional information
?
-
Saccharomyces cerevisiae VKM Y-1173
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
-
additional information
?
-
Escherichia coli CA10
-
contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-, Q8NRR8, Q8NT99
degradation of polyphosphate
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
h-prune efficiently hydrolyzes short-chain polyphosphates
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
-
regulatory enzyme in polyphosphate metabolism
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
show the reaction diagram
Saccharomyces cerevisiae CRY
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
ir
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
phosphate starvation induces the formation of the enzyme
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
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
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
show the reaction diagram
-
enzyme is derepressed under phosphate starvation conditions
-
-
?
additional information
?
-
Q6Y656, -
polyphosphates play a role in the parasite's osmoregulation, overview
-
-
-
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
-
-
-
additional information
?
-
-
PPN1 splitting long polyphosphate chains to shorter ones, PPX1 splitting off phosphate from the end of the polyphosphate chain
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Co2+
-
stimulated by divalent cations, Co2+ is the best stimulator, 6fold at 0.05 mM
Co2+
-
5 mM, 108% of the activation by Mg2+
Co2+
-
2 mM CoCl2, 2.5fold stimulation
Co2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Co2+
P38698, -
0.1 mM, 31fold activity enhancement; best activator
Co2+
-
0.1 mM, 6fold activity stimulation; 6fold activation at 0.1 mM
Co2+
-
little effect on polyP15 hydrolysis
Co2+
P0A840
KD: 46.9 +/- 5.66 micorM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Co2+
-
activates 4.4fold polyphosphatase II and activates 1.5fold polyphosphatase I both at 0.15 mM
Co2+
Q6Y656, -
activates
Co2+
-
2.5fold activation
Co2+
-
reaction requires a divalent metal cofactor
Co2+
-
0.1 mM Co2+, PPX activity is stimulated by a factor of two in the nuclear fraction, but not in the mitochondrial fraction
Cu2+
-
0.01 mM, stimulates
Fe2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Fe2+
-
5 mM, 34% of the activation by Mg2+
Fe2+
-, Q8NRR8, Q8NT99
enzyme is stimulated 0.26fold at a concentration of 2 mM
K+
P38698, -
100 mM, 30% activity enhancement; slight activation
K+
-
activates 2fold polyphosphatase II, but not activates polyphosphatase I
K+
-, Q8NRR8, Q8NT99
PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity
KCl
-
175 mM, stimulates
KCl
-
50 and 200 mM, 39 and 38% activity enhancement, respectively
Mg2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mg2+
-
1 mM, required
Mg2+
-
stimulates
Mg2+
-
required, optimal activity at 5 mM
Mg2+
-
1-10 mM, about 7fold activation
Mg2+
-
divalent cation required, Mg2+ is most effective
Mg2+
-
optimal activity of exopolyphosphatase II in presence of 3 mM
Mg2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
P38698, -
2.5 mM, 15fold activity enhancement
Mg2+
-
0.1 mM MgSO4, 5% activity loss; 1 mM, 2fold activity enhancement; 2fold activation at 0.1 mM
Mg2+
-
best activator at 1 mM using polyP3, polyP4 and polyP15 as substrates
Mg2+
P0A840
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ with 5'-AMP
Mg2+
Q97YV9, -
about 50% of the activity with Mn2+
Mg2+
Q6Y656, -
activates, preferred divalent cation
Mg2+
-
single tight binding site for Mg2+
Mg2+
-
1.6fold activation
Mg2+
-
reaction requires a divalent metal cofactor, bound substrate enhances enzyme affinity for the metal ion
Mg2+
-
2.5 mM Mg2+, PPX activity is stimulated by a factor of two in the nuclear fraction and in the mitochondrial fraction
Mg2+
-, Q8NRR8, Q8NT99
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
Mg2+
Q7Z032, -
dependent on
Mg2+
-
the activity of NMB1467 is dependent on Mg2+ with optimal activity observed with between 1 and 2 mM
Mn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mn2+
-
1-10 mM, 3-5fold stimulation
Mn2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
best activator for guanosine 5'-tetraphosphate hydrolysis
Mn2+
P0A840
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
Mn2+
Q97YV9, -
preferred divalent cation, required. Optimal concentration about 10 mM
Mn2+
Q6Y656, -
activates
Mn2+
-
reaction requires a divalent metal cofactor, Mn2+ confers 50% activity compared to Mg2+ in P3 and P4 hydrolysis
Mn2+
-, Q8NRR8, Q8NT99
enzyme is stimulated 0.86fold at a concentration of 2 mM
NaCl
-
50 and 200 mM, 46 and 42% activity enhancement, respectively
NH4+
P38698, -
100 mM, 35% activity enhancement; slight activation
NH4Cl
-
50 and 200 mM, 42 and 67% activity enhancement, respectively
Ni2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Ni2+
-
5 mM, 32% of the activation by Mg2+
Ni2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
P0A840
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
Zn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Zn2+
-
stimulates
Zn2+
-
0.1 mM ZnSO4, 76% activity loss; 1.5fold activation at 0.1 mM
Zn2+
-, Q8NRR8, Q8NT99
enzyme is stimulated 0.11fold at a concentration of 2 mM
Zn2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
Mn2+
-
0.5 mM, stimulates
additional information
-
exopolyphosphatase I does not require divalent cations
additional information
-
stimulated by divalent cations to a lesser extent
additional information
-
no activity measured in absence of divalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(phosphate)25
-
-
-
(phosphate)45
-
-
-
(phosphate)65
-
-
-
ADP
-
0.5 mM, 30% loss of activity, exopolyphosphatase II
ADP
-, Q8NRR8, Q8NT99
-
AlF4-
-
10 mM, 25% loss of activity
Ammonium molybdate
-
-
arginine
Q6Y656, -
inhibition of the recombinant enzyme at high concentrations
ATP
-
0.5 mM, 47% loss of activity, exopolyphosphatase II
ATP
-, Q8NRR8, Q8NT99
-
Ca2+
-
competitive with respect to Mg2+
Ca2+
-, Q8NRR8, Q8NT99
PPX2 is inhibited by millimolar concentrations
CaCl2
-, Q8NRR8, Q8NT99
3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
Cu2+
-
strong inhibitor
Cu2+
-
above 0.01 mM
dATP
-, Q8NRR8, Q8NT99
-
dGTP
-, Q8NRR8, Q8NT99
-
diphosphate
-
1 mM, 48% inhibition
diphosphate
-
competitive
diphosphate
-
1 mM, 24% activity loss; 25% inactivation at 1 mM
diphosphate
-
potential physiological regulator
dipyridamole
-
known inhibitor of phosphodiesterase, no effect on the triphosphate hydrolyzing activity of h-prune
dithiothreitol
-
0.1 mM, 13% activity loss
EDTA
-
exopolyphosphatase II
EDTA
-
0.1 mM, 100% activity loss; complete inactivation at 0.1 mM
EDTA
-
45% inhibition of polyphosphatase I and 55% inhibition of polyphosphatase II, both at 0.3 mM
GTP
-, Q8NRR8, Q8NT99
-
heparin
P38698, -
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 both low and high molecular mass enzymes
heparin
-
80% inhibition at 0.1 mM
heparin
-
complete inhibition of polyphosphatase I at 0.05 mg/ml, 35% inhibition of polyphosphatase II at 0.1 mg/ml
heparin
Q6Y656, -
inhibition of the recombinant enzyme at high concentrations
heparin
-
heparin (0.02 mg/ml) inhibits nuclear and mitochondrial PPX activity in about 90 and 95%
heparin
-
the activity is completely inhibited by 0.02 mg/ml heparin
hydrogen peroxide
-
-
iodoacetamide
-
10 mM, 2% inhibition
iodoacetamide
-
10 mM, 26% activity loss; 25% inactivation at 10 mM
ITP
-, Q8NRR8, Q8NT99
-
KCl
Q6Y656, -
slight inhibition at high concentrations
long-chain polyphosphate
-
potential physiological regulator, inhibits h-prune-catalyzed hydrolysis of triphosphate
-
lysine
Q6Y656, -
inhibition of the recombinant enzyme at high concentrations
MES buffer
-
20 mM
-
Mg2+
-
0.05 mM, 30% inhibition in a reaction mixture containing Co2+ at its optimal concentration
Mg2+
-
exopolyphosphatase I
Mg2+
-, Q8NRR8, Q8NT99
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 10 mM MnCl2
NaCl
-
400 mM, about 41% loss of activity
NaCl
-
600 mM NaCl, 73% inhibition of exopolyphosphatase I and 84% inhibition of exopolyphosphatase II
NaCl
Q6Y656, -
slight inhibition at high concentrations
NaF
-
10 mM, 20% inhibition
NaF
-
10 mM, 9% activity loss
NaF
-
selective inhibition of the high molecular mass enzyme
nm23-H1
-
metastasis suppressor protein, the exopolyphosphatase activity is suppressed
-
o-vanadate
-
10 mM, nearly complete inhibition
phosphate
-
no effect
Polyphosphate
-
polyP15, 50% inhibition at 200fold polymer molar excess over the long-chain polyphosphate substrate
polyphosphate 3
-
1mM, 4% activity loss
-
potassium cyanide
-
-
Pyrophosphate
-, Q8NRR8, Q8NT99
8.2 mM pyrophosphate leads to half-maximal inhibition of His-tagged PPX2
spermidine
-
0.17 mM, 50% loss of activity
Tetrapolyphosphate
-
50% inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
tripolyphosphate
-
weak inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
tripolyphosphate
-
1 mM, 62% inhibition
VO43-
-
1 mM, less than 5% reduced activity
Zn2+
-
0.05 mM, 71% inhibition in a reaction mixture containing Co2+ at its optimal concentration
Zn2+
-
strong inhibitor
Zn2+
Q7Z032, -
strong inhibitor
Mn2+
-, Q8NRR8, Q8NT99
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2
additional information
P38698, -
not inhibited by 1 mM sodium fluoride
-
additional information
-
not inhibited by antibodies suppressing the activity of 40 kDa-exopolyphosphatase
-
additional information
-
NaF and vanadate are not inhibitors
-
additional information
-
nucleoside triphosphates, diadenosine hexaphosphate, cAMP and dipyridamole do not affect the activity
-
additional information
Q7Z032, -
PPX1 is not inhibited by Ro-20-1724, sildenafil, zaprinast, papaverine or etazolate, or the sodium salts of vanadate, fluoride or sulfate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
50 mM, stimulates
ADP
-
slight stimulation
arginine
-
stimulates
carbonyl cyanide-4-trifluoromethoxyphenylhydrazone
-
-
-
dithiothreitol
-
about 50% stimulation of activity at 1 mM
NADH
-
2fold activation
polylysine
P38698, -
100 mg/l, 2fold activity enhancement
Pyruvic acid
-
activates PPX1, activation is inhibited KCN
succinic acid
-
activates PPX1, activation is inhibited KCN
KCl
-
150-300 mM
additional information
P38698, -
RNA does not alter the nuclear exopolyphosphatase activity
-
additional information
-
no activation by NAD+
-
additional information
-
nuclear polyphosphates decrease and activity of exopolyphosphatase increases after embryo cellularization until the end of embryogenesis
-
additional information
-, Q8NRR8, Q8NT99
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
-
additional information
Q7Z032, -
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.0069
-
(phosphate)25
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
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
0.0022
-
(phosphate)45
-
2 mM Mg2+ 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
-
0.0035
-
(Polyphosphate)n
-
n = 208, pH 7.2, 30C
0.025
-
(Polyphosphate)n
P38698, -
n = 208
0.075
-
(Polyphosphate)n
-
n = 15, pH 7.2, 30C
0.133
-
(Polyphosphate)n
P38698, -
n = 15
1.1
-
(Polyphosphate)n
-
n = 3, pH 7.2, 30C
26.8
-
(Polyphosphate)n
-
n = 4, pH 7.2
28.1
-
(Polyphosphate)n
-
n = 3, pH 7.2
39.1
-
(Polyphosphate)n
-
n = 15, pH 7.2
57.6
-
(Polyphosphate)n
-
n = 75, pH 7.2
1343
-
(Polyphosphate)n
-
n = 45, pH 7.2
0.1
-
3'-AMP
P0A840
+/- 0.01
0.37
-
3'-CMP
P0A840
+/- 0.08
0.32
-
5'-AMP
P0A840
+/- 0.04
0.28
-
5'-dGMP
P0A840
+/- 0.04
0.26
-
5'-GMP
P0A840
+/- 0.05
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
0.1
-
adenosine-5'-tetraphosphate
-
-
0.012
-
guanosine 5'-tetraphosphate
Q6Y656, -
pH 7.5, 30C
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
54.5
-
guanosine 5'-tetraphosphate
-
pH 7.2
2.49
-
p-nitrophenyl phosphate
P0A840
+/- 0.4
0.0272
-
pentasodium triphosphate
Q7Z032, -
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30C
-
0.0092
-
polyP10
-
exopolyphosphatase II
0.0238
-
polyP10
-
exopolyphosphatase I
2.4e-05
-
polyP100
-
-
0.0012
-
polyP208
-
-
0.0024
-
polyP208
-
-
0.00016
-
polyP25
-
-
0.0013
-
polyP33-36
-
-
-
0.033
-
polyP9-10
-
-
-
0.0035
-
Polyphosphate
-
208 phosphate residues, pH 7.2
0.02
-
Polyphosphate
P0A840
+/- 0.003
0.075
-
Polyphosphate
-
15 phosphate residues, pH 7.2
1.1
-
Polyphosphate
-
3 phosphate residues, pH 7.2
5
-
Polyphosphate
-
pH 7.2, 25C, recombinant wild-type enzyme
6
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant H149N
7.5
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant H148N
9
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant N35H
12
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant D127N
75
-
polyphosphate 15
-
-
-
3.5
-
polyphosphate 208
-
-
-
1100
-
polyphosphate 3
-
-
-
0.0022
-
sodium phosphate glass type 15
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28C
-
0.11
-
Tetraphosphate
-, Q8NRR8, Q8NT99
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.0002
-
Triphosphate
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28C
0.04
-
Triphosphate
-, Q8NRR8, Q8NT99
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.058
-
Triphosphate
Q6Y656, -
pH 7.5, 30C
0.14
-
tripolyphosphate
-
-
0.39
-
tripolyphosphate
-
-
0.41
-
tripolyphosphate
-
-
0.08
-
guanosine-5'-tetraphosphate
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
steady-state kinetic analysis
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
(phosphate)25
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
-
0.57
-
(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
13
-
(phosphate)3
-
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
35
-
(phosphate)3
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
3.4
-
(phosphate)4
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
7.1
-
(phosphate)4
-
2 mM Co2+ 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
-
1550
-
(Phosphate)n
-
37C, recombinant enzyme
9.84
-
3'-AMP
P0A840
+/- 0.37
5.93
-
3'-CMP
P0A840
+/- 0.44
4.9
-
5'-AMP
P0A840
+/- 0.3
8.04
-
5'-dGMP
P0A840
+/- 0.39
11
-
5'-GMP
P0A840
+/- 0.87
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
723
-
adenosine 5'-tetraphosphate
-
-
40
-
adenosine-5'-pentaphosphate
-
-
0.7
-
guanosine 5'-tetraphosphate
Q6Y656, -
pH 7.5, 30C
24
-
guanosine 5'-tetraphosphate
-
2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
3.55
-
p-nitrophenyl phosphate
P0A840
+/- 0.16
8.1
-
pentasodium triphosphate
Q7Z032, -
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30C
-
81
-
polyP33-36
-
-
-
90
-
polyP9-10
-
-
-
0.05
-
Polyphosphate
P0A840
+/- 0.005
0.14
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant D127N
0.52
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant H149N
0.66
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant H148N
2.2
-
Polyphosphate
-
pH 7.2, 25C, recombinant mutant N35H
1150
-
Polyphosphate
-
pH 7.2, 25C, recombinant wild-type enzyme
0.9
-
Tetraphosphate
-, Q8NRR8, Q8NT99
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
0.6
-
Triphosphate
-, Q8NRR8, Q8NT99
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
3.46
-
Triphosphate
Q6Y656, -
pH 7.5, 30C
143
-
tripolyphosphate
-
-
180
-
tripolyphosphate
-
-
27
-
guanosine 5'-tetraphosphate
-
2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
ADP
-, Q8NRR8, Q8NT99
-
2.6
-
ATP
-, Q8NRR8, Q8NT99
-
24.1
-
ATP
P0A840
with 3'-AMP as substrate
0.6
-
dATP
-, Q8NRR8, Q8NT99
-
0.4
-
dGTP
-, Q8NRR8, Q8NT99
-
0.8
-
GTP
-, Q8NRR8, Q8NT99
-
0.8
-
ITP
-, Q8NRR8, Q8NT99
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.163
-
(phosphate)25
-
2 mM Mg2+, 10 mM triphosphate
-
0.33
-
(phosphate)25
-
2 mM Mg2+, 100 mM triphosphate
-
0.055
-
(phosphate)45
-
2 mM Mg2+, 10 mM triphosphate
-
0.12
-
(phosphate)45
-
2 mM Mg2+, 100 mM triphosphate
-
0.064
-
(phosphate)65
-
c2 mM Mg2+, 10 mM triphosphate
-
0.105
-
(phosphate)65
-
c2 mM Mg2+, 100 mM triphosphate
-
1.2
-
diphosphate
-
2 mM Mg2+, 10 mM triphosphate
5.7
-
diphosphate
-
2 mM Mg2+, 100 mM triphosphate
0.0019
-
nm23-H1
-
2 mM Mg2+, 10 mM triphosphate
-
0.0072
-
nm23-H1
-
2 mM Mg2+, 10 mM triphosphate
-
0.0213
-
Zn2+
Q7Z032, -
in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30C
0.032
-
ZnCl2
-
2 mM Mg2+, hydrolysis of triphospate is inhibited
1
-
hydrogen peroxide
-
in 50 mM Tris-HCl buffer (pH 7.2), at 28C
additional information
-
nm23-H1
-
2 mM Mg2+, 60 microM (phosphate)25, 10 mM triphosphate, IC50 is above 0.01 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRX grown on lactate; membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.035
-
-
high-molecular weight exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.04
-
P38698, -
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
0.04
-
-, Q8NRR8, Q8NT99
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
0.05
-
P38698, -
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
-
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.08
-
-, Q8NRR8, Q8NT99
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
0.095
-
P38698, -
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
0.097
-
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.1
-
P38698, -
0.13 mM polyphosphate 15 as substrate, in the presence of 2.5 mM Mg2+
0.1
-
P0A840
+/- 0.01, polyphosphate
0.1
-
-
parent strain CRY, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.119
-
-
soluble form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.12
-
-, Q8NRR8, Q8NT99
wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2; 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
-
P38698, -
0.13 mM polyphosphate 15 as substrate, in the presence of 1 mM Co2+
0.23
-
P38698, -
0.13 mM polyphosphate 15 as substrate, in the presence of 0.1 mM Co2+
0.28
-
P38698, -
0.01 mM polyphosphate 208 as substrate, in the presence of 1 mM Co2+
0.3
-
P38698, -
2.0 mM polyphosphate 208 as substrate, in the presence of 0.1 mM Co2+
0.43
-
-, Q8NRR8, Q8NT99
overexpression of ppx1 increase the specific activity of exopolyphosphatase by 4fold compared to that of the empty vector control
0.47
-
-
enzyme from cystosol
0.8
-
-, Q8NRR8, Q8NT99
crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1
1.11
-
-
after ammonium sulfate precipitation
1.26
-
-
mitochondrial fraction
5
-
-
after DEAE-Toyopearl 650 M column chromatography
7.24
-
P0A840
+/- 0.34, p-nitrophenyl phosphate
10
-
P0A840
+/- 0.61, 5'-AMP
12.1
-
P0A840
+/- 0.90, 3'-CMP
16.4
-
P0A840
+/- 0.80, 5'-dGMP
20.1
-
P0A840
+/- 0.76, 3'-AMP
22.4
-
P0A840
+/- 1.78, 5'-GMP
150
-
-
after 319fold purification with heparin agarose, at 30C 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; pH 7.2, 30C, polyP208 as substrate
2070
-
-
purified recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
no specific activity on diphosphate, ATP and p-nitrophenyl phosphate
additional information
-
-
the exopolyphosphatase activity is reduced 6.5fold in the mutant CRN lacking endopolyphosphatase activity
additional information
-
-
polyphosphate levels in different cell compartments, overview
additional information
-
-
polyphosphate hydrolysis in the CRX strain cytosol completes in 120 min
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
-
-, Q8NRR8, Q8NT99
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
polyphosphatase I
4.8
-
-
in presence of Co2+
5
-
-
exopolyphosphatase I
6
6.5
-
and a second higher optimum at pH 7.5
6.5
-
-
hydrolysis of polyP3
6.8
-
-, Q8NRR8, Q8NT99
highest activity of recombinant His-tagged PPX2 is reached in 50 mM PIPES buffer
7
-
P0A840
-
7.5
-
-
and a second lower optimum at pH 6.0-6.5
7.5
-
-
exopolyphosphatase II
7.5
-
-
polyphosphatase II
7.5
-
Q6Y656, -
assay at
7.5
-
-
assay at
8
-
-
about
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
7.2
-
50% of maximal activity at pH 3.8 and at pH 7.2
4.6
5.4
-
pH 4.6: 81% of maximal activity, pH 5.4: 59% of maximal activity, exopolyphosphatase I
6
9
-
45-55% of maximal activity at pH 6.0 and at pH 9.0
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
Q6Y656, -
assay at
30
-
-, Q8NRR8, Q8NT99
-
50
60
Q97YV9, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
48
-
30C: about about 60% of maximal activity, 48C: about 40% of maximal activity
30
53
-
30C: about 30% of maximal activity, 53C: about 40% of maximal activity
70
-
Q97YV9, -
75% of maximum activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
Q7Z032, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
segmentation stage, 9th day after oviposition
Manually annotated by BRENDA team
Streptomyces aureofaciens RIA, Streptomyces aureofaciens RIA57
-
-
-
Manually annotated by BRENDA team
-
activity is 134% greater in mycorrhizal roots than in non-mycorrhizal roots of Allium cepa
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
-
; appears in the cytosol under PPX1 inactivation
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH22
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRY
-
PPN1
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae VKM Y-1173
-
-
-
Manually annotated by BRENDA team
-
nuclear exopolyphosphatase activity does not depend on the growth phase
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRX
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRY
-
PPN1
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRY
-
PPN1
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CRY
-
PPN1
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
additional information
-
no activity in the nuclear fraction
-
Manually annotated by BRENDA team
additional information
-
existence of 2 different PPX isoforms operating in the nuclei and mitochondria with distinct metal dependence, inhibitor and activator sensitivities
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Escherichia coli (strain K12)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
-
gel filtration
33000
-
-
SDS-PAGE, probably a product of mRNA splicing or/and protein processing
35000
-
-
gel filtration
40000
-
-
Sephacryl S-300 gel filtration
40000
-
-
exopolyphosphatase 1
42800
-
Q7Z032, -
SDS-PAGE
42870
-
Q7Z032, -
calculated from amino acid sequence
45000
-
-
exopolyphosphatase I, gel filtration
45000
-
-
about, PPX1
45000
-
-
determined by gel filtration
50000
-
-
estimated from the amino acid composition
55000
-
-
polyphosphatase II, gel filtration
58100
-
-
SDS-PAGE
70000
-
-
exopolyphosphatase II, gel filtration
78000
-
-
MALDI-TOF
93000
-
-
polyphosphatase I, gel filtration
100000
-
-
gel filtration
120000
830000
-
PPN1
125000
-
-
Superose 6 column gel filtration, active but unstable enzyme complex
200000
-
P38698, -
gel filtration; gel filtration on Superose 6
245000
-
-
gel filtration
450000
-
-
determined by gel filtration
500000
-
-
Superose 6 column gel filtration, stable enzyme complex composed of two polypeptides of 32 and 35 kDa and apparently polyphosphates
500000
-
-
Sephacryl S-300 gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
?
-
x * 48000, SDS-PAGE
?
Q97YV9, -
x * 47900, calculated
?
-
x * 45058, recombinant enzyme, mass spectrometry
?
-
x * 45000, SDS-PAGE
?
-, P65786
x * 36600, SDS-PAGE
?
Mycobacterium tuberculosis CDC 1551
-
x * 36600, SDS-PAGE
-
?
Saccharomyces cerevisiae VKM Y-1173
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
-
dimer
-
2 * 57000, SDS-PAGE; 2 * 58133, calculation from nucleotide sequence
dimer
-
x-ray crystallography
monomer
-
1 * 28000, SDS-PAGE
monomer
-
1 * 420000, SDS-PAGE
monomer
-
1 * 45000, exopolyphosphatase I, SDS-PAGE; 1 * 73000, exopolyphosphatase I, SDS-PAGE
monomer
P0A840
in solution
monomer
-, Q8NRR8, Q8NT99
determined by gel filtration
oligomer
P0A840
at least four subunits in solution
tetramer
-
4 * 55000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method
-
sitting drop vapour diffusion method
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
4C, 48 h, 95% loss of activity
5
-
-
4C, 48 h, 66% loss of activity
6
-
-
4C, 48 h, 21% loss of activity
7
-
-
4C, 48 h, 5% loss of activity
7.5
8
-
4C, 48 h, stable
9
-
-
4C, 48 h, 11% loss of activity
10
-
-
4C, 48 h, 95% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q8NRR8, Q8NT99
at pH 6.8, 2 mM MgCl2 and 25 mM KCl, no significant loss of activity is observed after 60 min
40
-
-
15 min, 70% loss of activity
45
-
-, Q8NRR8, Q8NT99
after preheating at 45C for 30 and 60 min, 70% and 40% of the PPX2 activity remains
50
-
-, Q8NRR8, Q8NT99
after preheating at 50C, His-tagged PPX2 loses its activity quickly, after incubation for 60 min, no activity remains
60
-
-
2 min, complete loss of activity, slight protection from heat inactivation, 10%, by 1 mM MnCl2
60
-
-, Q8NRR8, Q8NT99
complete inactivation of His-tagged PPX2 within 5 min
70
-
-
10 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity after dialysis
-
stable
P0A840
Mg2+ stabilizes h-prune against inactivation during storage
-
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
-
repeated freezing and thawing destroys activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for months
-
4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
P0A840
-80C, 300 mM NaCl, 250 mM sucrose, 2 mM dithiothreitiol, several months, no activity loss
-
-20C, 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
-
-4C, 0.1% Triton X-100, 1M KCl, 4 days, no activity loss
-
-4C, enzyme desorbed from heparin-agarose with 1 M KCl and 0.1% Triton X-100, 4 days, no loss of activity
-
4C, enzyme obtained by desorption with polyphosphate, 2 h, 30% loss of activity
-
4C, in absence of detergents, complete loss of activity after 24 h, can be stabilized by 0.1% Triton X-100 and protease inhibitors
-
92C, 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
-
92C, without 0.1% Triton X-100, 5 days, 66% loss of activity of the partially purified exopolyphosphatase preparation after DEAE-Toyopearl chromatography
-
-20C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant ppx2 enzyme is purified by Ni-nitrilotriacetic acid chromatography
-, Q8NRR8, Q8NT99
DEAE Sepharose filtration
-
HP-SP-Sepharose column chromatography
-
by metal chelate 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
Q9S605
DEAE-Toyopearl 650 M column chromatography; partial, using ion-exchange chromatography and gel filtration
-
gel filtration
-
ion-exchange chromatography
P38698, -
recombinant PPX1 17.4fold in a two-step procedure
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
exopolyphosphatase I and II
-
glutathione-Sepharose resin column chromatography or amylose-resin column chromatography
Q7Z032, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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; 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
-, Q8NRR8, Q8NT99
expressed in Escherichia coli as His-tagged wild type protein and His-tagged variants
-
expression in Escherichia coli of a his-tagged recombinant enzyme
-
expressed in Escherichia coli Arctic Express (DE3) cells
-, P65786
expression in Escherichia coli
Q9S605
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene PPX1, overexpression
-
expression in Escherichia coli
Q97YV9, -
expressed in Escherichia coli BL21(DE3) cells
Q7Z032, -
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3)
Q6Y656, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D143A
-
single amino acid mutation of Ppx
E121A
-
single amino acid mutation of Ppx
E150A
-
single amino acid mutation of Ppx
E371A
-
single amino acid mutation of Ppx
D106A
-
variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
D179A
-
variant is inactive
D28A
-
variant is inactive
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
N24H
-
variant is inactive
R128H
-
enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold
R348A
-
variant is inactive
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
N35H
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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
Saccharomyces cerevisiae AH22
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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
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D127N
Saccharomyces cerevisiae AH22
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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
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H149N
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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
additional information
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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
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mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme
additional information
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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
H148N
Saccharomyces cerevisiae AH22
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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
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additional information
Saccharomyces cerevisiae AH22
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mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme
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N35H
Saccharomyces cerevisiae AH22
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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
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additional information
Saccharomyces cerevisiae CRY
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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
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additional information
Q6Y656, -
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