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Information on EC 3.1.1.72 - acetylxylan esterase and Organism(s) Neocallimastix patriciarum and UniProt Accession B8YG19

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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:
Neocallimastix patriciarum
UNIPROT: B8YG19
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Word Map
The taxonomic range for the selected organisms is: Neocallimastix patriciarum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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
bifunctional acetylxylan esterase/xylanase
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Acetic ester hydrolase
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-
-
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Acetyl esterase
-
-
-
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Acetylglucomannan esterase
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-
-
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Acetylnaphthylesterase
-
-
-
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Acetyte esterase
-
-
-
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C-esterase
-
-
-
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Chloroacetate esterase
-
-
-
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Chloroesterase
-
-
-
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Citrus acetylesterase
-
-
-
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Esterase, acetyl
-
-
-
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Esterase, C-
-
-
-
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Heroin esterase
-
-
-
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N-Acetylphosphinothricin deacetylase
-
-
-
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Naphthal AS-D chloroacetate deacetylase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Deacetylation of xylans and xylo-oligosaccharides
show the reaction diagram
catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-naphthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
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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
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9000-82-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
show the reaction diagram
-
-
-
?
acetylxylan + H2O
?
show the reaction diagram
-
-
-
?
beechwood xylan + H2O
?
show the reaction diagram
-
-
-
?
beta-D-xylose tetraacetate + H2O
?
show the reaction diagram
-
-
-
?
birchwood xylan + H2O
?
show the reaction diagram
-
-
-
?
oat spelt xylan + H2O
?
show the reaction diagram
-
-
-
?
acetylated xylan + H2O
xylan + acetate
show the reaction diagram
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substrate prepared from birchwood, the recombinant enzyme acts synergistically with xylanase to degrade acetylated xylan
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.72
birchwood xylan
pH 8.2, 58°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1228
acetylxylan esterase activity on beta-D-xylose tetraacetate, pH 8.2, 58°C, purified recombinant enzyme
2614
acetylxylan esterase activity on acetylxylan, pH 8.2, 58°C, purified recombinant enzyme
273.7
acetylxylan esterase activity on birchwood xylan, pH 8.2, 58°C, purified recombinant enzyme
557.9
acetylxylan esterase activity on oat spelt xylan, pH 8.2, 58°C, purified recombinant enzyme
580.3
acetylxylan esterase activity on 4-methylumbelliferyl acetate, pH 8.2, 58°C, purified recombinant enzyme
873.1
acetylxylan esterase activity on beechwood xylan, pH 8.2, 58°C, purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
carbohydrate esterase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
carbohydrate esterase activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene xynS20E
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XS20E_NEOPA
671
0
72469
Swiss-Prot
Secretory Pathway (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
gene bnaA, recombinant His-tagged enzyme from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of a bifunctional acetylxylan esterase/xylanase, XynS20E, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strain BL21
gene bnaA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli as His-tagged protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cybinski, D.H.; Layton, I.; Lowry, J.B.; Dalrymple, B.P.
An acetylxylan esterase and a xylanase expressed from genes cloned from the ruminal fungus Neocallimastix patriciarum act synergistically to degrade acetylated xylans
Appl. Microbiol. Biotechnol.
52
221-225
1999
Neocallimastix patriciarum
Manually annotated by BRENDA team
Pai, C.; Wu, Z.; Chen, M.; Zeng, Y.; Chen, J.; Duan, C.; Li, M.; Liu, J.
Molecular cloning and characterization of a bifunctional xylanolytic enzyme from Neocallimastix patriciarum
Appl. Microbiol. Biotechnol.
85
1451-1462
2010
Neocallimastix patriciarum (B8YG19), Neocallimastix patriciarum, Neocallimastix patriciarum S20 (B8YG19)
Manually annotated by BRENDA team