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Literature summary for 3.6.1.11 extracted from

  • Tammenkoski, M.; Moiseev, V.M.; Lahti, M.; Ugochukwu, E.; Brondijk, T.H.; White, S.A.; Lahti, R.; Baykov, A.A.
    Kinetic and mutational analyses of the major cytosolic exopolyphosphatase from Saccharomyces cerevisiae (2007), J. Biol. Chem., 282, 9302-9311.
    View publication on PubMed
Search for more literature for 3.6.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
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 Saccharomyces cerevisiae
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 Saccharomyces cerevisiae
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 Saccharomyces cerevisiae
H149N 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 Saccharomyces cerevisiae
additional information mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
N35H 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 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetic analysis Saccharomyces cerevisiae
5
-
 Polyphosphate pH 7.2, 25°C, recombinant wild-type enzyme Saccharomyces cerevisiae
6
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant H149N Saccharomyces cerevisiae
7.5
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant H148N Saccharomyces cerevisiae
9
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant N35H Saccharomyces cerevisiae
12
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant D127N Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Saccharomyces cerevisiae 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ single tight binding site for Mg2+ Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae AH22
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(phosphate)n + H2O
-
 Saccharomyces cerevisiae (phosphate)n-1 + phosphate
-
 ?
(phosphate)n + H2O
-
 Saccharomyces cerevisiae AH22 (phosphate)n-1 + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
More PPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase, PPase Saccharomyces cerevisiae
PPX
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.14
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant D127N Saccharomyces cerevisiae
0.52
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant H149N Saccharomyces cerevisiae
0.66
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant H148N Saccharomyces cerevisiae
2.2
-
 Polyphosphate pH 7.2, 25°C, recombinant mutant N35H Saccharomyces cerevisiae
1150
-
 Polyphosphate pH 7.2, 25°C, recombinant wild-type enzyme Saccharomyces cerevisiae

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
4.2 9.5
-
 Saccharomyces cerevisiae