3.6.1.11: exopolyphosphatase
This is an abbreviated version!
For detailed information about exopolyphosphatase, go to the full flat file.
Word Map on EC 3.6.1.11
Reaction
Synonyms
40 kD exopolyphosphatase, 40-kDa-exopolyphosphatase, acid phosphoanhydride phosphohydrolase, CJJ81176_0377, CJJ81176_1251, CT0099, CT1713, ecPpx, exopoly(P)ase, ExopolyPase, exopolyphosphatase, exopolyphosphatase 1, exopolyphosphatase 2, Gra-Pase, h-prune, high molecular mass exopolyphosphatase, high molecular weight exopolyphosphatase, high-molecular exopolyphosphatase, LmPPX, major cytosolic exopolyphosphatase PPX1, membrane-bound exopolyphosphatase, metaphosphatase, More, Msed_0981, MT0516, NMB1467, nuclear exopolyphosphatase, Nudix hydrolase, paPpx, phosphatase, exopoly-, polyphosphate phosphatase, polyphosphate phosphohydrolase, polyphosphate-phosphohydrolase, Ppn1, PPX, Ppx protein, Ppx/GppA phosphatase, PPX1, PPX2, PPXI, PPXMsed, Rv0496, Tb927.5.4350, Tb927.6.2670, TbDcp2, TbNH2, TbNH4, vacuolar exopolyphosphatase, YHR201C, Za10_0559, ZmPPX
ECTree
3.6.1.11 exopolyphosphataseAdvanced search results
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results (Engineering
Engineering on EC 3.6.1.11 - exopolyphosphatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D106A
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variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
H107N
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variant displays reduced activity with a turnover value of 4.4% compared to the wild type counterpart, Km value increases 7fold
H108N
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variant displays reduced activity with a turnover value of 32% compared to the wild type counterpart
R128H
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enhanced kcat value (146%) is obtained with the mutant protein compared to the wild type counterpart, Km value increases 21fold
E112A
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
E112A
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site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
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E112A
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site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
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E112A
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site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
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E112A
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site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
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E112A
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site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
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D127E
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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
D127N
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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
H148N
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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
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
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
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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
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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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H148N
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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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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
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E137A
additional information
E137A
site-directed mutagenesis of the truncated mutant ZmPPX(30-508), an active site mutant
E137A
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site-directed mutagenesis of the truncated mutant ZmPPX(30-508), an active site mutant
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additional information
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construction of a truncated enzyme mutants comprising amino acid residues 1-314 of 506 (N-paPpx(1-314)), or residues 1-303 (N-paPpx(1-303)), or residues 315-506 (C-paPpx(315-506)) of paPpx, amplified from Pseudomonas aeruginosa wild-type strain PAO1 chromosomal DNA through PCR. Only paPpx(1-506) and N-paPpx(1-314) are enzymatically active, while C-paPpx(315-506) lacks enzymatic activity
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
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
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
additional information
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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
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
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additional information
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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
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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
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additional information
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
additional information
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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
additional information
truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
additional information
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truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
additional information
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truncation of 29 amino acids from the N-terminus of the enzyme protein of mutant ZmPPX(30-508) results in a significant improvement in the diffraction of ZmPPX crystals from 3.3 to 1.8 A resolution using synchrotron radiation
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