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
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3.1.1.72
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xylans
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cellulase
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wheat
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biomass
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xylose
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aspergillus
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trichoderma
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pulp
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straw
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lignocellulosic
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bran
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xylooligosaccharides
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cellulolytic
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endoglucanase
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xylanolytic
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rumen
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pectinase
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reesei
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bagasse
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arabinoxylans
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saccharification
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birchwood
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lignin
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xylotriose
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laccase
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cmcase
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spelt
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digesta
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hemicellulases
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stover
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avicel
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cellulose-binding
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phytase
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beta-xylosidase
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cellulosome
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thermomyces
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naphthol
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thermocellum
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mannanase
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lignocellulolytic
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cellobiohydrolase
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feruloylated
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fibrolytic
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kraft
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lanuginosus
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delignification
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degradation
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carbohydrase
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synthesis
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medicine
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biofuel production
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cellulomonas
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beta-glucanase
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analysis
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cellobiase
- 3.1.1.72
- xylans
- cellulase
- wheat
- biomass
- xylose
- aspergillus
- trichoderma
- pulp
- straw
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lignocellulosic
- bran
- xylooligosaccharides
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cellulolytic
- endoglucanase
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xylanolytic
- rumen
- pectinase
- reesei
- bagasse
- arabinoxylans
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saccharification
-
birchwood
- lignin
- xylotriose
- laccase
- cmcase
- spelt
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digesta
-
hemicellulases
- stover
- avicel
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cellulose-binding
- phytase
- beta-xylosidase
- cellulosome
- thermomyces
- naphthol
- thermocellum
- mannanase
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lignocellulolytic
- cellobiohydrolase
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feruloylated
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fibrolytic
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kraft
- lanuginosus
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delignification
- degradation
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carbohydrase
- synthesis
- medicine
- biofuel production
- cellulomonas
- beta-glucanase
- analysis
- cellobiase
Reaction
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
3.1.1.72 acetylxylan esteraseAdvanced search results
results (
results (Engineering
Engineering on EC 3.1.1.72 - acetylxylan esterase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D168A
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kcat/Km for alpha-naphthylacetate is 1.7fold lower than the wild-type value
D202A
S146A
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mutant enzyme shows lower specific activity towards the C2 substrate and higher thermal stability than wild-type enzyme. the lower activity is due to a combination of increased Km and decreased kcat. The catalytic efficiency of the mutant is 41% lower than that of wild-type enzyme
W160P
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
W160S
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
Y39A
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
Y39G
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
Y39G/W160P
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
Y39P
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
Y39P/W160S
significant decrease in the activity for the acetyl substrate,increase in activity for longer chain substrates
S181A
D270A
displays catalytic activity against tetraacetyl-xylopyranoside
D270N
displays catalytic activity against tetraacetyl-xylopyranoside
E194A
displays some catalytic activity
E194A/D270A
activity is completely abolished
E194N
exhibits detectable catalytic activity
H273Q
activity is completely abolished
S44G
activity is completely abolished
Y184F/W190P
A4D
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random mutagenesis, altered mutant deacetylation activity on acetylated oligosaccharides compared to the wild-type enzyme
D12A
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no activity with acetylated xylan, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 6.5% of the wild-type activity, activity with N,N'-diacetylchitobiose is 4.5% of the wild-type activity
D12N
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activity with acetylated xylan is 3.2% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 8.1% of the wild-type activity, activity with N,N'-diacetylchitobiose is 6.3% of the wild-type activity
D130A
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no activity with acetylated xylan, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 11.2% of the wild-type activity, activity with N,N'-diacetylchitobiose is 6.5% of the wild-type activity
D130E
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activity with acetylated xylan is 27.7% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 14.3% of the wild-type activity, activity with N,N'-diacetylchitobiose is 6.1% of the wild-type activity
D130N
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no activity with acetylated xylan, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 7.0% of the wild-type activity, activity with N,N'-diacetylchitobiose is 5.1% of the wild-type activity
D130Q
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activity with acetylated xylan is 10% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 12.1% of the wild-type activity, activity with N,N'-diacetylchitobiose is 5.4% of the wild-type activity
D13A
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no activity with acetylated xylan, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 7.8% of the wild-type activity, activity with N,N'-diacetylchitobiose is 8.6% of the wild-type activity
D156A
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activity with acetylated xylan is 42% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 41.4% of the wild-type activity, activity with N,N'-diacetylchitobiose is 48.6% of the wild-type activity
D156E
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activity with acetylated xylan is 81.7% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 50.8% of the wild-type activity, activity with N,N'-diacetylchitobiose is 56.7% of the wild-type activity
D156N
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activity with acetylated xylan is 52.5% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 35.8% of the wild-type activity, activity with N,N'-diacetylchitobiose is 24.2% of the wild-type activity
D156Q
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activity with acetylated xylan is 63.2% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 36.6% of the wild-type activity, activity with N,N'-diacetylchitobiose is 19.6% of the wild-type activity
H155A
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activity with acetylated xylan is 5.2% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 9.9% of the wild-type activity, activity with N,N'-diacetylchitobiose is 2.8% of the wild-type activity
H62A
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activity with acetylated xylan is 13.2% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 10.3% of the wild-type activity, activity with N,N'-diacetylchitobiose is 4.2% of the wild-type activity
H66A
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activity with acetylated xylan is 30.5% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 8.3% of the wild-type activity, activity with N,N'-diacetylchitobiose is 3.5% of the wild-type activity
H68A
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activity with acetylated xylan is 94.9% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 36% of the wild-type activity, activity with N,N'-diacetylchitobiose is 35.1% of the wild-type activity
Q30E
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random mutagenesis, altered mutant deacetylation activity on acetylated oligosaccharides compared to the wild-type enzyme
S63A/H66A
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activity with acetylated xylan is 63.9% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 11.9% of the wild-type activity, activity with N,N'-diacetylchitobiose is 5.0% of the wild-type activity
S63A/H66D
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activity with acetylated xylan is 32.9% of the wild-type activity, activity with methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside is 5.5% of the wild-type activity, activity with N,N'-diacetylchitobiose is 4.4% of the wild-type activity
N96S/F210L
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mutant is more thermostable but less active than wild-type
additional information
D202A
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mutant shows greater synthetic activity of ethyl n-hexanoate as compared with the wild-type. kcat/Km for alpha-naphthylacetate is 1.5fold higher than the wild-type value
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
Y184F/W190P
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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
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additional information
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fusion of family 3 carbohydrate binding module CBM3 from Clostridium thermocellum to the carboxyl terminus of the acetyl xylan esterase. CBM3 fusion has negligible impact on the thermostability or regioselectivity of AXE, activities towards acetylated corncob xylan, 4-methylumbelliferyl acetate, 4-nitrophenyl acetate, and cellobiose octaacetate are also unchanged. The activity of the fusion protein on cellulose acetate is 4fold increased compared with wild-type
additional information
presence of two additional amino acid residues at the enzyme's native N-terminus help stabilize the enzyme against the protease cleavages without affecting the enzyme activity
additional information
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presence of two additional amino acid residues at the enzyme's native N-terminus help stabilize the enzyme against the protease cleavages without affecting the enzyme activity
additional information
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presence of two additional amino acid residues at the enzyme's native N-terminus help stabilize the enzyme against the protease cleavages without affecting the enzyme activity
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additional information
truncational mutant proteins TM1 (esterase domain plus carbohydrate-binding module), TM2 (esterase domain), TM3 (carbohydrate-binding module plus FPm-1 domain), TM4 (carbohydrate-binding module) and TM5 (FPm-1 domain). Truncation of FPm-1 leads to a dramatic reduction of binding activity for the TM1 mutant. TM1 and TM2 have no discernible affinity for insoluble oat spelt xylan, whereas TM3, TM4, and TM5 bind to this substrate
additional information
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truncational mutant proteins TM1 (esterase domain plus carbohydrate-binding module), TM2 (esterase domain), TM3 (carbohydrate-binding module plus FPm-1 domain), TM4 (carbohydrate-binding module) and TM5 (FPm-1 domain). Truncation of FPm-1 leads to a dramatic reduction of binding activity for the TM1 mutant. TM1 and TM2 have no discernible affinity for insoluble oat spelt xylan, whereas TM3, TM4, and TM5 bind to this substrate
additional information
WP_024831741
construction of derivatives Abf62A-Axe6A, containing all four modules but lacking the signal peptide, Abf62A-CBM6, containing the GH62 and CBM6 modules and Axe6A, containing only family 6 catalytic module CE6. Both Abf62A-Axe6A and RjAxe6A show acetylxylan esterase activities, Abf62A-Axe6 exhibits a higher activity toward insoluble wheat arabinoxylan compared with Axe6
additional information
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construction of derivatives Abf62A-Axe6A, containing all four modules but lacking the signal peptide, Abf62A-CBM6, containing the GH62 and CBM6 modules and Axe6A, containing only family 6 catalytic module CE6. Both Abf62A-Axe6A and RjAxe6A show acetylxylan esterase activities, Abf62A-Axe6 exhibits a higher activity toward insoluble wheat arabinoxylan compared with Axe6
additional information
Ruminiclostridium josui JCM 1788
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construction of derivatives Abf62A-Axe6A, containing all four modules but lacking the signal peptide, Abf62A-CBM6, containing the GH62 and CBM6 modules and Axe6A, containing only family 6 catalytic module CE6. Both Abf62A-Axe6A and RjAxe6A show acetylxylan esterase activities, Abf62A-Axe6 exhibits a higher activity toward insoluble wheat arabinoxylan compared with Axe6
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additional information
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development method of random mutagenesis of the gene axeAtr encoding the catalytic subunit for directed evolution of Streptomyces lividans acetyl xylan esterase to obtain chitooligosaccharides with well-defined structural properties, overview. The long term goal of this multidisciplinary approach is to improve the activity of chitosan oligosaccharides to an industrially applicable level
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
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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
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
