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Information on EC 3.1.1.72 - acetylxylan esterase and Organism(s) Volvariella volvacea and UniProt Accession Q09IZ4
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3.1.1.72 acetylxylan esteraseIUBMB 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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Word Map
- 3.1.1.72
- xylans
- cellulase
- wheat
- biomass
- xylose
- aspergillus
- trichoderma
- pulp
- straw
-
lignocellulosic
- bran
- xylooligosaccharides
-
cellulolytic
- endoglucanase
-
xylanolytic
- rumen
- pectinase
- reesei
- bagasse
- arabinoxylans
-
saccharification
-
birchwood
- lignin
- xylotriose
- laccase
- cmcase
- spelt
-
digesta
-
hemicellulases
- stover
- avicel
-
cellulose-binding
- phytase
- beta-xylosidase
- cellulosome
- thermomyces
- naphthol
- thermocellum
- mannanase
-
lignocellulolytic
- cellobiohydrolase
-
feruloylated
-
fibrolytic
-
kraft
- lanuginosus
-
delignification
- degradation
-
carbohydrase
- synthesis
- medicine
- biofuel production
- cellulomonas
- beta-glucanase
- analysis
- cellobiase
The taxonomic range for the selected organisms is: Volvariella volvacea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
xylanase, chloroacetate esterase, acetyl xylan esterase, acetyl esterase, xyn10b, acetylxylan esterase, axe ii, axe i, ca esterase, xyns20e, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
188959-24-2
-
9000-82-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
-
?
acetylated xylan + H2O
xylan + acetate
exhibits activity toward acetylated oat spelt xylan
-
-
?
additional information
?
-
alpha-naphthyl acetate is a poor substrate for the enzyme and is hydrolyzed at only 1.8% of the rate observed with xylose tetraacetate. No activity is detectable on p-nitrophenyl acetate
-
-
?
additional information
?
-
-
alpha-naphthyl acetate is a poor substrate for the enzyme and is hydrolyzed at only 1.8% of the rate observed with xylose tetraacetate. No activity is detectable on p-nitrophenyl acetate
-
-
?
additional information
?
-
exhibits activity toward various chitinous substrates, but is totally inactive against 4-methylumbelliferyl acetate, beta-nitrophenyl acetate, xylose tetraacetate, and alpha-naphthyl acetate
-
-
?
additional information
?
-
-
exhibits activity toward various chitinous substrates, but is totally inactive against 4-methylumbelliferyl acetate, beta-nitrophenyl acetate, xylose tetraacetate, and alpha-naphthyl acetate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
is required for catalysis. Enzyme activity increases by 54% on addition of 0.1 mM
Mg2+
is required for catalysis. 1-10 mM slightly enhance enzyme activity by 11-12%
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
concentrations greater than 1 mM almost eliminate the activity, but simultaneous addition of Co2+ (1 mM) and Mg2+ (1 mM) restores the activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
papain
-
enzyme activity is increased by 17-29% by 0.001 mg/0.05 ml papain
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.079
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM6, pH 8.0, 50°C
0.087
4-methylumbelliferyl acetate
wild-type lacking CBM1, 50°C, pH 8.0
0.094
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM22-2, pH 8.0, 50°C
0.099
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM4-2, pH 8.0, 50°C
additional information
additional information
1.42 mg/mL with glycol chitin as substrate, in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min
-
additional information
additional information
-
1.42 mg/mL with glycol chitin as substrate, in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
485
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM6, pH 8.0, 50°C
485
4-methylumbelliferyl acetate
wild-type lacking CBM1, 50°C, pH 8.0
562
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM22-2, pH 8.0, 50°C
897
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM4-2, pH 8.0, 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5590
4-methylumbelliferyl acetate
wild-type lacking CBM1, 50°C, pH 8.0
5970
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM22-2, pH 8.0, 50°C
6170
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM6, pH 8.0, 50°C
9090
4-methylumbelliferyl acetate
mutant carrying a replacement of CBM1 with CBM4-2, pH 8.0, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min: 3448 IU/micromol with acetylated xylan as substrate, 830.9 IU/micromol with glycol chitin as substrate, 306.7 IU/micromol with chitosan as substrate, 361.1 IU/micromol with colloidal chitin as substrate
additional information
-
in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min: 3448 IU/micromol with acetylated xylan as substrate, 830.9 IU/micromol with glycol chitin as substrate, 306.7 IU/micromol with chitosan as substrate, 361.1 IU/micromol with colloidal chitin as substrate
additional information
-
23373 U/l/mol and 22692 U/l/mol are obtained for the wild-type and endo-H-treated enzyme forms, and 23306 U/l/mol, 23026 U/l/mol, and 22605 U/l/mol are recorded for the enzyme obtained from yeast cultures supplemented with 0.002, 0.0055 and 0.010 mg/ml tunicamycin, respectively
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 10
pH 7.5: about 40% of maximal activity, pH 10: about 40% of maximal activity, hydrolysis of 4-methylumbelliferyl acetate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
30°C: about 50% of maximal activity, 70°C: about 90% of maximal activity, hydrolysis of 4-methylumbelliferyl acetate
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the enzyme has two potential N-linked glycosylation sites. N-linked glycosylation plays an essential role in enzyme secretion but has only a slight effect on the catalytic activity and stability of the recombinant enzyme. Deglycosylation of purified recombinant wild-type enzyme using endoglycosidase H at pH 5.5, 28°C, for 12 h
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of fusion proteins with xylan-specific CBM4-2, CBM6, and CBM22-2 modules from Rhodothermus marinus Xyn10A, Clostridium thermocellum Xyn11A, and Clostridium thermocellum Xyn10B, respectively. Replacement of CBM1 with xylan-specific CBM4-2 significantly enhances AXE1 thermostability and catalytic activity against substrate 4-methylumbelliferyl acetate. Replacements with CBM6 and CBM22-2 are more effective in enzymatic release of acetic acid from destarched wheat bran, NaClO2-treated wheat straw, and water-insoluble wheat arabinoxylan compared to AXE1. Replacement with CBM6 and CBM22-2 also results in higher degree releases of reducing sugar and acetic acid from different substrates
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
endo-H-treated enzyme and enzyme from tunicamycin-supplemented yeast cultures are marginally less stable on prolonged exposure to 50°C, pH values below 9.0, and urea concentrations above 2.0 M compared with the wild-type enzyme
730875
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
90 min, 3% residual activity for wild-type, 40% residual activity for mutant carrying a replacement of CBM1 with CBM4-2
50
-
endo-H-treated enzyme and enzyme from tunicamycin-supplemented yeast cultures are marginally less stable on prolonged exposure to 50°C, pH values below 9.0, and urea concentrations above 2.0 M compared with the wild-type enzyme
50 - 60
is very stable at 60°C and, after a 6 h incubation at 50°C, over 95% of the activity remains
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
endo-H-treated enzyme and enzyme from tunicamycin-supplemented yeast cultures are marginally less stable on prolonged exposure to 50°C, pH values below 9.0, and urea concentrations above 2.0 M compared with the wild-type enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AXEII with the 6-histidine tag purified by affinity chromatography using Ni-NTA column
untreated recombinant enzyme and recombinant enzyme from tunicamycin-supplemented cultures are purified by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length cDNA or 5'-end DNA fragment subcloned into the pGEM-T vector. Full-length gene encoding the mature esterase fused with a 6-histidine tag attached at the C-terminal and ligated at the EcoR1/Xba1 sites of the Picchia pastoris expression vector pPICZaA to yield the construct pPICZaA-AXEII. Transformed and expressed in Pichia pastoris
gene axe1, recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H using a codon-optimized axe1 synthesized by the primer extension PCR procedure, method optimization by response surface methodology, e.g. BMMY medium with 2.8% methanol, 0.63% casamino acids, and pH 8.0, overview. The enzyme is secreted
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
axeII transcript levels are high when the fungus is grown on oat spelt xylan (highest level), cellobiose, microcrystalline cellulose, carboxymethyl-cellulose, lactose, galactose, and chitin from crab as carbon sources
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ding, S.; Cao, J.; Zhou, R.; Zheng, F.
Molecular cloning, and characterization of a modular acetyl xylan esterase from the edible straw mushroom Volvariella volvacea
FEMS Microbiol. Lett.
274
304-310
2007
Volvariella volvacea (Q09IZ4), Volvariella volvacea, Volvariella volvacea V14 (Q09IZ4)
Liu, X.; Ding, S.
Molecular characterization of a new acetyl xylan esterase (AXEII) from edible straw mushroom Volvariella volvacea with both de-O-acetylation and de-N-acetylation activity
FEMS Microbiol. Lett.
295
50-56
2009
Volvariella volvacea (B8YIE0), Volvariella volvacea, Volvariella volvacea V14 (B8YIE0)
Tian, B.; Chen, Y.; Ding, S.
A combined approach for improving alkaline acetyl xylan esterase production in Pichia pastoris, and effects of glycosylation on enzyme secretion, activity and stability
Protein Expr. Purif.
85
44-50
2012
Volvariella volvacea
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