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3.6.1.7: acylphosphatase

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

Word Map on EC 3.6.1.7

Reaction

an acylphosphate
+
H2O
=
a carboxylate
 +
phosphate

Synonyms

1,3-diphosphoglycerate phosphatase, acetic phosphatase, acetyl phosphatase, acetylphosphatase, ACP, AcPDRo2, acyl phosphatase, acyl phosphate phosphohydrolase, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, erythrocyte/testis isozyme, Acylphosphate phosphohydrolase, acylphosphate phosphomonohydrolase, Acyp, ACYP2, carbamoylphosphate phosphatase, carbamyl phosphate phosphatase, Ch1, Ch2, GP 1-3, GP1, GP2, GP3, Ho 1-3, Ho1, Ho2, Ho3, human common-type acylphosphatase, Isozyme CH1, Isozyme CH2, Isozyme TU1, More, muscle-type acylphosphatase 2, native acylphosphatase, PhAcP, phosphatase, acyl, Sso AcP, SSO0887, T1, TT0497

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.7 acylphosphatase

Crystallization

Crystallization on EC 3.6.1.7 - acylphosphatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
common-type enzyme, resolution of 1.8 A
-
crystals belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8 A, c = 98.6 A, gamma = 120°, refinement to 1.5 A resolution
-
vapour diffusion method
-
muscle enzyme, not suitable for X-ray diffraction
-
sitting drop vapour diffusion method using polyethylene glycol 4000 as precipitant
-
muscular isoenzyme
-
not suitable for X-ray diffraction
-
sitting drop vapour diffusion
-
sitting drop vapour diffusion method with potassium/sodium tartrate at pH 5.5
-
sitting drop vapour diffusion method with sodium formate as precipitant
-
sitting-drop vapour-diffusion method using sodium formate as precipitant at 16°C. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65 A, c = 75.51 A. The asymmetric unit contains two molecules of enzyme
-
sitting-drop vapour-diffusion method with postasium/sodium tartrate as the precipitant at pH 5.5. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.7 A, c = 75.4 A and two monomers in the asymmetric unit
-
sitting-drop-vapor-diffusion method, 1.5 A crystal structure. The enzyme forms a dimer in the crystal structure via antiparallel association of strand 4
sitting-drop-vapor-diffusion with sodium formate as precipitant at pH 6.0
the structure of G91A mutant enzyme is determined by x-ray crystallography at 2.4 A resolution, and it is superimposable with the structure of wild-type enzyme
resolution to 1.27 and 1.9 A
-
sitting drop vapour diffusion, crystal structures of mutant enzymes V84D, Y86E and V84P are determined
vapour diffusion method
-
not suitable for X-ray diffraction
-
skeletal muscle enzyme
-
purified recombinant TT0497, 0.0005 ml of 2.9 mg/ml protein in 20 mM Tris-HCl pH 8.0, 0.2 M NaCl is mixed with 0.0005 ml of precipitant solution containing 27.5% w/v PEG 4000 and 0.1 M MES, pH 6.9, X-ray diffraction structure determination and analysis at 1.3 A resolution, structural refinement based on the Fourier method, modelling, overview