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3.1.8.1: aryldialkylphosphatase

This is an abbreviated version!
For detailed information about aryldialkylphosphatase, go to the full flat file.

Word Map on EC 3.1.8.1

Reaction

An aryl dialkyl phosphate
+
H2O
=
dialkyl phosphate
 +
an aryl alcohol

Synonyms

A-esterase, A7Q26_23485, aminopeptidase P, AMPP, aryldialkylphosphatase, arylesterase, aryltriphosphatase, bacterial phosphotriesterase, DFPase, diisopropyl fluorophosphatase, esterase B1, esterase E4, esterase, organophosphate, esterase, paraoxon, esterase, pirimiphos-methyloxon, G3C9 rePON1, h-PON1, HAD, haloalkylphosphorus hydrolase, HDL-associated esterase/lactonase paraoxonase 1, HDL-PON1, high activity paraoxonase, high-density lipoprotein-associated esterase/lactonase, human paraoxonase 1, HuPON1, inner membrane protein YiaH, lactonase SsoPox, lactonase/phosphotriesterase, low activity paraoxonase, methyl parathion hydrolase, More, Mph, mPHP, OP hydrolase, OP-hydrolase, OP-hydrolyzing enzyme, OPA anhydrase, opd, OpdA, OpdD, OPH, OPHC2, organophosphate hydrolase, organophosphorous hydrolase, organophosphorus acid anhydrase, organophosphorus hydrolase, organophosphorus pesticide hydrolase, organophosphorus-hydrolyzing enzyme, paraoxon hydrolase, paraoxonase, paraoxonase 1, paraoxonase 1A, paraoxonase 3, paraoxonase-1, paraoxonase-2, paraoxonase1, parathion hydrolase, phosphotriesterase, phosphotriesterase homology protein, phosphotriesterase-like lactonase, PHP, pirimiphos-methyloxon esterase, PLL, PO.ase, PON, PON 1, PON-1, PON-aryl, PON-para, PON1, PON1A, PON2, PON3, POX, PTE, PTE S5, Rv0230c, SACI2140, Saci_2140, SacPox, Sb-PTE, serum paraoxonase, serum paraoxonase 1, SisLac, SisPox, Sso, SSO2522, SsoPox, type A paraoxonase, type B paraoxonase, VmoLac, Vmut2255, VmutPLL

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.8 Phosphoric-triester hydrolases
                3.1.8.1 aryldialkylphosphatase

Crystallization

Crystallization on EC 3.1.8.1 - aryldialkylphosphatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with Co2+, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 6.4 mg/ml protein in 50 mM Hepes, pH 7.0, 150 mM NaCl, and 1 mM CoCl2, are mixed with 0.005 ml of reservoir solution that consists of 20% w/v PEG 3350 and 0.2 M sodium nitrate, X-ray diffraction structure determination and analysis at 1.9 A resolution
hanging drop vapour diffusion method, in 10% PEG6000, 0.1 M HEPES, pH 7.0, 1% diethyl 4-methylbenzylphosphonate, and 5 mM sodium azide
in complex with diisopropyl methyl phosphonate and with triethyl phosphate
-
purified recombinant enzyme mutants A80V/F132V/K185R/H254Q/H257Y/I274N/S308L and I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L, vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM HEPES, pH 8.5, and 1.0 mM CoCl2, with 0.001 ml of precipitant solution containing 100 mM sodium cacodylate, pH 5.5-7.0, 0.2 M magnesium acetate, and 15-30% PEG 8000, and equilbration against 0.5 ml of the precipitant solution, 7-21 days, 18°C, X-ray diffraction structure determination and analysis, molecular replacement using the coordinates of wild-type PTE, PDB ID 1DPM, as the search model
purified recombinant mutant enzyme H254R bound to inhibitor diethyl 4-methylbenzylphosphonate, 5.8 mg/ml protein in 20 mM HEPES, pH 7.5, hanging drop vapour diffusion method, room temperature, the precipitation solution contains 9% PEG 6000, 100 mM CHES, pH 9.0, 1% diethyl 4-methylbenzylphosphonate, and 5 mM sodium azide, no Co2+ is added, X-ray diffraction structure determination and analysis at 1.9 A resolution
in the presence of Co2+, by vapor diffusion method in hanging drop, to 2.36 A resolution. The active site contains three substrate binding pockets: the small (F28, Y30, T70, C74, V268, and W271), large (R230, I233, M236, V237, and W289) and leaving group (Y100 and E103) pockets. Metal binding site contains a tyrosine residue at position 97 in close proximity to the beta-metal
-
purified recombinant wild-type and selenomethionine-labeled PON1 genetic variant G2E6 by use of different mother liquors, microbatch method, X-ray diffracion structure determination and analysis at 2.2-2.6 A resolution
purified recombinant enzyme mutant G137D, hanging drop vapor diffusion method, the reservoir solution contains 100 mM sodium-acetate, pH 4.6, and 20% PEG 2000 monomethyl ester, 17°C, X-ray diffraction structure determination and analysis at 2.01 A resolution, molecular replacement using the previously determined structure of LcalphaE7, PDB ID 4FNG, as template, model building
-
purified recombinant N-terminally His6-tagged enzyme with bound Zn2+, X-ray diffraction structure determination and analysis at 2.3 A resolution, the first residue of the N-terminal (Met1) and the last residue of the C-terminal (Gln326) are missing due to the lack of density. Molecular replacement, the structure of phosphotriesterase from Sulfolobus solfataricus (SsoPox), PDB ID 2VC5, is used as the search model
to 2.1 A resolution, monoclinic space group C2, with unit-cell parameters a = 109.9, b = 63.8, c = 221.3 A, beta = 101.8°
crystal structure analysis of SsoPox in the apo form and in complex with a quorum-sensing lactone mimic at 2.6 and 2.0A resolution, respectively, overview
hanging drop vapour diffusion method
purified recombinant enzyme, hanging-drop vapour-diffusion technique, 5.8 mg/ml protein in 20 mM HEPES, pH 8.5, 0.2 mM CoCl2 and 0.2 M NaCl, 0.001-0.002 ml of protein and reservoir solutions are mixed and equilibrated against 0.8 ml reservoir solution containing 15-18% w/v PEG 8000 and 50 mM Tris-HCl buffer pH 8.0, 1 week at 4°C, X-ray diffraction structure determination and analysis at 2.54 A resolution
-
purified recombinant wild-type enzyme and mutant asA6 in open conformation, asA6 in closed conformation, asB5, asC6, asD6, and asA1, hanging drop vapor diffusion method, mixing of 500 nl protein solution, containing protein in 50 mM HEPES, pH 8.0, 150 mM NaCl, and 0.2 mM CoCl2, and 500 nl reservoir solution, containing 20-30% w/v PEG 8000, and 50 mM Tris-HCl, pH 8.0, a few days, 4°C, X-ray diffraction structure determination and analysis at 1.4-2.95 A resolution
sitting-drop vapour-diffusion method at 20°C, 2.34 A resolution
phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6
-
protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another
-
sitting drop vapor diffusion method at 20°C, X-ray structures of the enzyme bound to a fatty acid and to its substrate acyl-homoserine lactone