Any feedback?
Information on EC 3.1.1.72 - acetylxylan esterase and Organism(s) Talaromyces purpureogenus and UniProt Accession Q8NJP6
for references in articles please use BRENDA:EC3.1.1.72Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Talaromyces purpureogenus
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
-
-
-
-
acetyl xylan esterase II
Acetylglucomannan esterase
-
-
-
-
Acetylnaphthylesterase
-
-
-
-
Acetyte esterase
-
-
-
-
AXE II
C-esterase
-
-
-
-
Chloroacetate esterase
-
-
-
-
Chloroesterase
-
-
-
-
Citrus acetylesterase
-
-
-
-
Esterase, acetyl
-
-
-
-
Esterase, C-
-
-
-
-
Heroin esterase
-
-
-
-
N-Acetylphosphinothricin deacetylase
-
-
-
-
Naphthal AS-D chloroacetate deacetylase
-
-
-
-
additional information
additional information
-
enzyme belongs to carbohydrate esterase family 1
additional information
-
enzyme belongs to carbohydrate esterase family 5
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Deacetylation of xylans and xylo-oligosaccharides
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, reaction mechanism, catalytic triad consists of Ser90, His187, and Asp175
Deacetylation of xylans and xylo-oligosaccharides
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.
-
Deacetylation of xylans and xylo-oligosaccharides
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.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
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-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
acetylated xylan + H2O
xylan + acetate
acetate esters of D-xylanopyranose residues in xylan substrates
-
?
cellulose acetate + H2O
cellulose + acetate
-
cleavage of acetyl at position C2
-
?
additional information
?
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
additional information
?
-
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
additional information
?
-
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.3
-
with substrate 4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
1.7
-
with substrate 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
2.7
-
with substrate 4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
3.06
-
with substrate 4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
3.4
-
with substrate 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
36.2
-
with substrate 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
5.5 - 6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme expression from gene axeII is strictly regulated by the pH value, axeII transcript appears only at neutral pH
additional information
-
enzyme expression from gene axeII is strictly regulated by the pH value, axeII transcript appears only at neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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). AXE1_TALPU
382
0
40273
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
preparation of a deletion mutant where the amino acid 104-114 are eliminated. This mutant is catalytically active and can hydrolyze long chain fatty acid esters with much greater efficiency than the wild type AXE II
additional information
-
preparation of a deletion mutant where the amino acid 104-114 are eliminated. This mutant is catalytically active and can hydrolyze long chain fatty acid esters with much greater efficiency than the wild type AXE II
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
mutant enzyme is less stable than the native recombinant protein at 70°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
acetylxylan esterase II, 67% residue identity with the acetylxylan esterase I from Trichoderma reesei
native and mutant protein is expressed in Aspergillus nidulans A722
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Egana, L.; Gutierrez, R.; Caputo, V.; Peirano, A.; Steiner, J.; Eyzaguirre, J.
Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum
Biotechnol. Appl. Biochem.
24
33-39
1996
Talaromyces purpureogenus
Gutierrez, R.; Cederlund, E.; Hjelmqvist, L.; Peirano, A.; Herrera, F.; Ghosh, D.; Duax, W.; Jrnvall, H.; Eyzaguirre, J.
Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain
FEBS Lett.
423
35-38
1998
Trichoderma reesei, Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
Chavez, R.; Schachter, K.; Navarro, C.; Peirano, A.; Bull, P.; Eyzaguirre, J.
The acetyl xylan esterase II gene from Penicillium purpurogenum is differentially expressed in several carbon sources, and tightly regulated by pH
Biol. Res.
37
107-113
2004
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
Ghosh, D.; Sawicki, M.; Lala, P.; Erman, M.; Pangborn, W.; Eyzaguirre, J.; Gutierrez, R.; Jornvall, H.; Thiel, D.J.
Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A
J. Biol. Chem.
276
11159-11166
2001
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
Altaner, C.; Saake, B.; Tenkanen, M.; Eyzaguirre, J.; Faulds, C.B.; Biely, P.; Viikari, L.; Siika-aho, M.; Puls, J.
Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families
J. Biotechnol.
105
95-104
2003
Talaromyces purpureogenus, Schizophyllum commune, Streptomyces lividans, Trichoderma reesei
Colombres, M.; Garate, J.A.; Lagos, C.F.; Araya-Secchi, R.; Norambuena, P.; Quiroz, S.; Larrondo, L.; Perez-Acle, T.; Eyzaguirre, J.
An eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from Penicillium purpurogenum
J. Comput. Aided Mol. Des.
22
19-28
2008
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
Gordillo, F.; Caputo, V.; Peirano, A.; Chavez, R.; Van Beeumen, J.; Vandenberghe, I.; Claeyssens, M.; Bull, P.; Ravanal, M.C.; Eyzaguirre, J.
Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene
Mycol. Res.
110
1129-1139
2006
Talaromyces purpureogenus (Q8NJP6), Talaromyces purpureogenus
Biely, P.; Mastihubova, M.; Tenkanen, M.; Eyzaguirre, J.; Li, X.L.; Vrsanska, M.
Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of beta-D-xylopyranose and alpha-L-arabinofuranose
J. Biotechnol.
151
137-142
2011
Talaromyces purpureogenus, Schizophyllum commune, Streptomyces lividans, Trichoderma reesei
EXTERNAL LINKS (specific for EC-Number 3.1.1.72)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
