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3.1.1.6: acetylesterase

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

Word Map on EC 3.1.1.6

Reaction

An acetic ester
+
H2O
=
an alcohol
 +
acetate

Synonyms

6-O-deacetylase, ACE, AcE1, acetate ester-hydrolysing esterase, acetic acid esterase, Acetic ester hydrolase, Acetyl esterase, acetyl xylan esterase, acetyl-esterase, acetylesterase CE16, AE, AE206, Aes, Aes1, alpha/beta-acetylesterase, Axe3, BS2, C-esterase, C20orf3, carbohydrate acetylesterase, carbohydrate esterase, CE16, CE16 acetyl esterase, CE16A, CE2, CE2A, CE2B, CE2C, Chloroesterase, Citrus acetylesterase, EST-4, Est1, EST2, Est24, ESTK, GAE, geranyl acetate cleaving esterase, haemagglutinin-esterase, HE, HerE, More, non-specific acetyl esterase, p-nitrophenyl acetate esterase, PAE1, PAE11, PAE2, PAE3, PAE4, PAE5, PAE6, PAE7, PAE8, PAE9, pectin acetylesterase, ragi acetic acid esterase, TM0077, ybaC

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.6 acetylesterase

Crystallization

Crystallization on EC 3.1.1.6 - acetylesterase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamic simulations and automated docking with R and S enantiomers of substrate 1,1,1-trifluoro-2-phenyl-but-3-yn-1-yl acetate using structure of wild-type and structural model of double mutant E188W/M193C, S enantiomer fits better in active site of mutant E188W/M193C because subtrates phenyl group points out of it, docking of the preferred R enantiomer by the wild-type with lower free energy than docking of the S enantiomer
-
His-tagged protein, both in the native form and with selenomethionine substitution
-
structural superimposition of homology-generated model with Alicyclobacillus acidocaldarius EST2 and Escherichia coli beta-cystathionase MalY revealed nine amino acid consensus sequence putatively involved in protein-protein interactions, amino acids 178-184 are putative core of interaction with MalY and MalT
-
structural modelling using Cn3D 4.1 software and plant strictosidine synthase as model structure, six-bladed beta-propeller structure
-
purified selenomethionine enzyme, 6-7 mg/ml, pure or complexed with the inhibitor dimethylarsinic acid, crystal growth in 1.8 M ammonium sulfate, 0.1 M NaCl, 0.1 M cacodylate, pH 6.5, for crystallization of native methionine enzyme 1.7 M ammonium sulfate, 0.1 M NaCl, 0.1 M BES, pH 6.4, is used, X-ray structure determination and analysis at 1.3 A and 1.45 A resolution
-
using 0.2 M ammonium phosphate (pH 4.6), and 20% (w/v) polyethylene glycol 3350
hanging drop vapor diffusion method, using 170 mM ammonium sulfate, 28% (w/v) PEG 4000, 5% (v/v) glycerol and 0.5% (w/v) n-octyl-beta-D-glucopyranoside
-
S10A mutant enzyme complexed with an acetate ion, sitting drop vapor diffusion method, using 0.1 M MES buffer (pH 6.5), 15-20% (v/v) PEGME 550, and 10 mM ZnSO4
-
hanging drop vapor diffusion method, using 20% (w/v) PEG-3000, 0.1 M HEPES pH 7.5, 0.2 M NaCl (selenomethionine-substituted enzyme) or nanodrop vapor diffusion method, using 0.2 M calcium acetate hydrate, 20% (w/v) PEG 3350, pH 7.3 at 20°C (native enzyme)
-