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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

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

Crystallization

Crystallization on EC 3.6.1.11 - exopolyphosphatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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
-
purified recombinant detagged wild-type enzyme by hanging drop vapour diffusion, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris, pH 8.0, 500 mM NaCl, and 5% glycerol, with 0.001 ml of reservoir solution containing 15.2% w/v PEG 3350, 2% w/v PEG 8000, 72 mM Tris, pH 8.0, 144 mM magnesium chloride hexahydrate, 20 mM HEPES/sodium hydroxide pH 7.5, 1.6% v/v glycerol, and 8% v/v DMSO, and equilibration against 0.2 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 3.3 A resolution. Purified recombinant detagged mutant truncated enzyme and truncated mutant E137A by sitting drop vapour diffusion, mixing of 0.001 ml of 8 mg/ml protein in 50 mM Tris, pH 8.0, 500 mM NaCl, and 5% glycerol, with 0.001 ml of reservoir solution containing 0.2 M magnesium chloride hexahydrate, 0.1 M Tris, pH 8.5 or pH 6.5, respectively, 25% w/v PEG 3350, and equilibration against 0.1 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.80 and 1.56 A resolution, respectively. Molecular replacement