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

(Polyphosphate)n
+
H2O
=
(polyphosphate)n-1
+
phosphate

Synonyms

More, metaphosphatase, phosphatase, exopoly-, acid phosphoanhydride phosphohydrolase, Gra-Pase, exopoly(P)ase, ExopolyPase, PPX, Ppn1, LmPPX, h-prune, nuclear exopolyphosphatase, high molecular mass exopolyphosphatase, polyphosphate phosphohydrolase, high molecular weight exopolyphosphatase, 40 kD exopolyphosphatase, polyphosphate-phosphohydrolase, major cytosolic exopolyphosphatase PPX1, vacuolar exopolyphosphatase, exopolyphosphatase 1, exopolyphosphatase 2, PPXI, membrane-bound exopolyphosphatase, 40-kDa-exopolyphosphatase, high-molecular exopolyphosphatase, polyphosphate phosphatase, Ppx protein, PPX1, Nudix hydrolase, exopolyphosphatase, PPX2, NMB1467, MT0516, CT0099, CT1713, CJJ81176_0377, CJJ81176_1251, Rv0496, paPpx, TbNH4, TbDcp2, Tb927.6.2670, TbNH2, Tb927.5.4350, YHR201C, ZmPPX, Za10_0559, PPXMsed, Ppx/GppA phosphatase, Msed_0981, ecPpx

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.11 exopolyphosphatase

Engineering

Engineering on EC 3.6.1.11 - exopolyphosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
D28A
-
variant is inactive
D179A
-
variant is inactive
D106A
-
variant displays reduced activity with a turnover value of 35% compared to the wild type counterpart
H107N
-
variant displays reduced activity with a turnover value of 4.4% compared to the wild type counterpart, Km value increases 7fold
N24H
-
variant is inactive
H108N
-
variant displays reduced activity with a turnover value of 32% compared to the wild type counterpart
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
E111A
site-directed mutagenesis, inactive mutant
E113A
site-directed mutagenesis, inactive mutant
E112A
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
E111A
-
site-directed mutagenesis, inactive mutant
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
E111A
-
site-directed mutagenesis, inactive mutant
-
E113A
-
site-directed mutagenesis, inactive mutant
-
E112A
-
site-directed mutagenesis, the mutant shows unaltered PPX activity compared to wild-type
-
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
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
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
-
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
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
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
-
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
-
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
-
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
-
E137A
additional information