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Information on EC 3.1.1.72 - acetylxylan esterase and Organism(s) Geobacillus stearothermophilus and UniProt Accession Q09LX1

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.72 acetylxylan esterase
IUBMB Comments
Catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: Q09LX1
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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acetylxylan
+
3
H2O
=
3
acetic acid
+
xylan
+
3
=
3
+
Synonyms
xylanase, chloroacetate esterase, acetyl xylan esterase, acetyl esterase, xyn10b, acetylxylan esterase, axe ii, axe i, xyns20e, acetyl xylan esterase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl xylo-oligosaccharide esterase
-
Acetic ester hydrolase
-
-
-
-
Acetyl esterase
-
-
-
-
Acetylglucomannan esterase
-
-
-
-
Acetylnaphthylesterase
-
-
-
-
Acetyte esterase
-
-
-
-
C-esterase
-
-
-
-
Chloroacetate esterase
-
-
-
-
Chloroesterase
-
-
-
-
Citrus acetylesterase
-
-
-
-
Esterase, acetyl
-
-
-
-
Esterase, C-
-
-
-
-
Heroin esterase
-
-
-
-
N-Acetylphosphinothricin deacetylase
-
-
-
-
Naphthal AS-D chloroacetate deacetylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetylxylan esterase
Catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
CAS REGISTRY NUMBER
COMMENTARY hide
188959-24-2
-
9000-82-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
acetylxylan esterases hydrolyse the ester linkages of the xylan acetyl groups and thus improve the ability of main-chain hydrolysing enzymes to break down the sugar backbone units. As such, these enzymes play an important part in the hemi-cellulolytic utilization system of many microorganisms that use plant biomass for growth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AXE2_GEOSE
219
0
24772
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
the wild-type enzyme is present as a unique torus-shaped octamer in the crystal and in solution
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y184F/W190P
site-directed mutagenesis, a dimeric enzyme mutant that shows a significant reduction in catalytic activity compared to the wild-type enzyme, structure comparison with the wild-type, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant mutant Y184F/W190P from Escherichia coli strain BL21(DE3) by protamine precipitation and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene axe2, expression in Escherichia coli strain B834(DE3) for synthesis of a selenomethionine-labeled enzyme, and in strain BL21(DE3) for synthesis of the wild-type enzyme
gene axe2, overexpression of mutant Y184F/W190P in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lansky, S.; Alalouf, O.; Solomon, V.; Alhassid, A.; Govada, L.; Chayen, N.E.; Chayan, N.E.; Belrhali, H.; Shoham, Y.; Shoham, G.
Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus
Acta Crystallogr. Sect. F
69
430-434
2013
Geobacillus stearothermophilus (Q09LX1), Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6 (Q09LX1)
Manually annotated by BRENDA team
Lansky, S.; Alalouf, O.; Salama, R.; Dvir, H.; Shoham, Y.; Shoham, G.
Preliminary crystallographic analysis of a double mutant of the acetyl xylo-oligosaccharide esterase Axe2 in its dimeric form
Acta Crystallogr. Sect. F
70
476-481
2014
Geobacillus stearothermophilus (Q09LX1), Geobacillus stearothermophilus T-6 (Q09LX1)
Manually annotated by BRENDA team