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Literature summary for 3.6.1.11 extracted from

  • Andreeva, N.; Ledova, L.; Ryazanova, L.; Tomashevsky, A.; Kulakovskaya, T.; Eldarov, M.
    Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae Comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases (2019), Biochimie, 163, 101-107 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene ppx1, recombinant overexpression in Saccharomyces cerevisiae strain CRN Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
heparin inhibits the endopolyphosphatase activity by 50% at 0.05 mg/ml Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0033
-
cAMP pH 7.2, 30°C, recombinant enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P38698
-
-
Saccharomyces cerevisiae ATCC 204508 P38698
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme PPX1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
240
-
purified recombinant enzyme, pH 7.2, 30°C Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cAMP + H2O
-
Saccharomyces cerevisiae adenosine + phosphate
-
?
cAMP + H2O
-
Saccharomyces cerevisiae ATCC 204508 adenosine + phosphate
-
?
diphosphate + H2O only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 Saccharomyces cerevisiae 2 phosphate
-
?
diphosphate + H2O only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1 Saccharomyces cerevisiae ATCC 204508 2 phosphate
-
?
GTP + H2O
-
Saccharomyces cerevisiae GDP + phosphate
-
?
GTP + H2O
-
Saccharomyces cerevisiae ATCC 204508 GDP + phosphate
-
?
guanosine tetraphosphate + H2O
-
Saccharomyces cerevisiae guanosine triphosphate + phosphate
-
?
guanosine tetraphosphate + H2O
-
Saccharomyces cerevisiae ATCC 204508 guanosine triphosphate + phosphate
-
?
additional information Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain Saccharomyces cerevisiae ?
-
-
additional information Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain Saccharomyces cerevisiae ATCC 204508 ?
-
-
polyphosphate208 + H2O
-
Saccharomyces cerevisiae ?
-
?
polyphosphate3 + H2O
-
Saccharomyces cerevisiae diphosphate + phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 45050, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
exopolyphosphatase
-
Saccharomyces cerevisiae
PPX1
-
Saccharomyces cerevisiae
YHR201C locus name Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the enzyme belongs to the DHH family of phosphoesterases. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast Saccharomyces cerevisiae
metabolism the enzyme PPN1 shows only exopolyphosphatase activity Saccharomyces cerevisiae