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3.1.1.72: acetylxylan esterase

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

Word Map on EC 3.1.1.72

Reaction

acetylxylan
+ 3 H2O = 3 acetic acid +
xylan

Synonyms

Abf62A-Axe6A, Acel_0180, Acetic ester hydrolase, acetyl (xylan) esterase, Acetyl esterase, acetyl xylan esterase, acetyl xylan esterase 1, acetyl xylan esterase 2, acetyl xylan esterase A, acetyl xylan esterase I, acetyl xylan esterase II, acetyl xylan esterase, putative, acetyl xylan esterase/cephalosporin acetyl hydrolase, acetyl xylo-oligosaccharide esterase, Acetylglucomannan esterase, Acetylnaphthylesterase, acetylxylan esterase, acetylxylan esterase A, Acetyte esterase, AcXE, AE, alkaline acetyl xylan esterase, An12 g05010, AoAXE, AXE, AXE I, AXE II, AXE/CAH, Axe1, Axe2, Axe3, Axe6A, Axe6B, AxeA, AXEII, bifunctional acetylxylan esterase/xylanase, BnaA, C-esterase, CA esterase, CE1, CE1 AcXE, CE2, CE3, CE4, CE4 AcXE, CE5, CE5 AcXE, CE6, CE6 AcXE, Chloroacetate esterase, Chloroesterase, Citrus acetylesterase, CtAxe, DFP58_4623, Est2A, Esterase, acetyl, Esterase, C-, Heroin esterase, More, N-Acetylphosphinothricin deacetylase, NaM1, Naphthal AS-D chloroacetate deacetylase, PcAxe2, SlCE4, Vvaxe1, xylanase, Xyn10B, XynA, XynS20E

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.72 acetylxylan esterase

Crystallization

Crystallization on EC 3.1.1.72 - acetylxylan esterase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fragment encoding the CE4 domain in complex with Cd2+, Mg2+ or Co2+, vapour-diffusion hanging-drop method
-
catalytic machinery includes a catalytic triad (Ser119, His259, and Asp202) and an oxyanion hole (Cys40 and Ser120). Near the catalytic triad, aromatic residues Tyr39 and Trp160 form small pockets at both sides
purified recombinant enzyme free or in complex with paraoxon or diethyl phosphate, sparse matrix sitting drop vapour diffusion sampling procedure, 21°C, mixing of 0.0004 ml of protein solution, containing 8 mg/ml protein in 0.05 M Tris-HCl, pH 8.0, alone or supplemented with 0.5 mM paraoxon, with 0.0004 ml of reservoir solution containing 0.2 M MgCl2, 0.1 M HEPES, pH 7.5, and 30% w/v PEG 400, for enzyme in complex with diethyl phosphate, 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 45% v/v 2-methyl-2,4-pentanediol is used as the crystallization solution, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution, molecular replacement
recombinant wild-type enzyme, hanging drop vapor diffusion method, in a micro-batch experiment. Rod-like diffraction quality crystals are obtained using 10% PEG 6000, 0.1 M MES pH 6.0 and a wide range of LiCl concentrations (0.2-1.0 M) as precipitating agent. Two different crystal forms, bith belonging to space group P2(1), are characterized, diffracting X-rays to 2.5 and 1.9 A resolution. 12 molecules in the asymmetric unit of either crystal forms are arranged as two doughnut-like hexamers, each one encompassing a local 32 symmewtry. Catalytic inactive mutant S181A is also crystallized
-
purified recombinnat wild-type enzyme and mutant H351A, X-ray diffraction structure determination and analysis at 2.1 A and 2.0 A resolution, respectively, single wavelength anomalous diffraction and molecular replacement methods, three-dimensional structure determintaion
purified recombinant enzyme mutant Y184F/W190P, hanging drop vapour diffusion method, mixing of 0.0025 ml of 3 mg/ml protein in 50 mM Tris–HCl pH 7.0, 100 mM NaCl, and 0.02% NaN3, with 0.0025 ml of reservoir solution containing 16-21% PEG 3000, 0.1 M Tris-HCl, pH 7.5, and 200 mM calcium acetate, and equilibration over 0.5-1.0 ml reservoir solution, method optimization, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant wild-type and selenomethionine-labeled enzyme, mixing of 0.0025 ml of 3-6 mg/ml protein solution with 0.0025 ml of reservoir solution, and equilibration against 1 ml of reservoir solution, 4 different conditions resulting in four different crystal forms, best conditions are obtained with 6 mg/ml protein and 1.2 M K tartrate, 0.3 M NaCl, 0.1 M imidazole buffer, pH 7.2, 1-3 days, X-ray diffraction structure determination and analysis at 1.70-1.85 A resolution, three-dimensional structure determination
AcE forms a hexamer with a central substrate binding tunnel, and the intersubunit interactions are relatively weak. AcE also has a shorter loop and different residue composition in the beta4-alpha3 and beta5-alpha4 regions near the substrate binding site
-
fragment encoding the CE4 domain, vapour-diffusion hanging-drop method
-
protein solution: ammonium sulfate in 50 mM citrate buffer, pH 5.3, X-ray diffraction structure determination at 0.9 and 1.1 A, analysis of the multiple conformations of the active site residues Ser90 and His187
structure is determined by X-ray crystallography at 0.9 resolution
purified catalytic core of the enzyme at 10 mg/ml, hanging drop vapour diffusion method, room temperature, protein solution: sodium acetate, pH 5.0, reservoir solution: potassium/sodium tartrate 1.1 M, TES buffer 0.1 M, pH 8.2, in the ratio 2:1:1 with a Trixton X-100 solution, few weeks, X-ray diffraction structure determination and analysis at 1.9 A, structure model