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evolution
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the enzyme belongs to aspartate-metalloesterase carbohydrate esterase family 4, CE4
evolution
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the enzyme belongs to aspartate-metalloesterase carbohydrate esterase family 4, CE4
evolution
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the enzyme belongs to carbohydrate esterase family 7
evolution
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the enzyme belongs to serine-type esterase carbohydrate esterase family 1, CE1
evolution
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the enzyme belongs to serine-type esterase carbohydrate esterase family 5, CE5
evolution
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the enzyme belongs to serine-type esterase carbohydrate esterase family 6, CE6
evolution
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the enzyme belongs to the carbohydrate esterase family 1, CE1
evolution
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the enzyme belongs to the carbohydrate esterase family 1, CE1
evolution
the enzyme belongs to the carbohydrate esterase family 2, CE2, and has a domain structure typical of CE2 family structures, a C-terminal SGNH domain and an N-terminal jelly-roll domain
evolution
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the enzyme belongs to the carbohydrate esterase family 5, CE5
evolution
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the enzyme belongs to the carbohydrate esterase family CE1
evolution
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the enzyme belongs to the carbohydrate esterase family CE1
evolution
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the enzyme belongs to the carbohydrate esterase family CE5
evolution
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the enzyme belongs to the carbohydrate esterase family 1, CE1
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evolution
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the enzyme belongs to carbohydrate esterase family 7
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evolution
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the enzyme belongs to the carbohydrate esterase family 2, CE2, and has a domain structure typical of CE2 family structures, a C-terminal SGNH domain and an N-terminal jelly-roll domain
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metabolism
white rot fungus Phanerochaete chrysosporium is capable of degrading woody biomass by enzymatic processes. Biomass degradation by this fungus is accomplished through a complex mixture of cellulases, hemicellulases and ligninases. Its putative xylan-degrading system involves xylanases, acetyl xylan esterases, alpha-L-arabinofuranosidases, and glucuronyl esterases (alpha-D-glucuronidase)
metabolism
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white rot fungus Phanerochaete chrysosporium is capable of degrading woody biomass by enzymatic processes. Biomass degradation by this fungus is accomplished through a complex mixture of cellulases, hemicellulases and ligninases. Its putative xylan-degrading system involves xylanases, acetyl xylan esterases, alpha-L-arabinofuranosidases, and glucuronyl esterases (alpha-D-glucuronidase)
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physiological function
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acetyl xylan esterase is an enzyme that catalyzes the hydrolysis of acetyl side groups from glucuronoxylan, which is the main component of hardwood hemicelluloses
physiological function
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acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases
physiological function
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acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases
physiological function
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acetylxylan esterases enhance the hydrolysis of O-acetylated xylan by removing the acetyl substituents that restrict the action of endo-1,4-beta-xylanases and beta-xylosidases
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
physiological function
the synergistic action of Axe2 with endo-xylanase XynC on birchwood xylan, beechwood xylan and wheat arabinoxylan enhances the total reducing soluble sugar
physiological function
expression in Arabidopsis thaliana. The protein is targeted to the apoplast by its native signal peptide, resulting in elevated acetyl esterase activity in soluble and wall-bound protein extracts and reduced xylan acetylation. No significant alterations in cell wall composition are observed. The xylans of transgenic lines are more easily digested by a beta-1,4-endoxylanase, and more readily extracted by hot water, acids or alkali. Transgenic plants develop normally and show increased resistance to the biotrophic pathogen Hyaloperonospora arabidopsidis
physiological function
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overexpression in Trichoderma reesei by fusing with xylanase Xyn2 from Trichoderma reesei as a carrier protein. The production of AXE in the transformant T2 is approximately 74% higher than that of the parent strain. The saccharification efficiency of rAXE gives approximately 23.2%, 22.7%, and 19.4% higher yield of reducing sugar in paddy straw, corn stover plus paddy straw mix (1:1 ratio), and corn stalk (delignified) hydrolysis
physiological function
sequence reveals a GH62 domain exhibiting alpha-L-arabinofuranosidase activity, in addition to the expected esterase domain
physiological function
WP_024831741
wild-type is a trifunctional xylanolytic enzyme exhibiting alpha-L-arabinofuranosidase, endoxylanase, and acetylxylan esterase activities
physiological function
Xyn10B is a trifunctional enzyme having endoxylanase, arabinofuranosidase and acetyl xylan esterase activities. Xyn10B is highly active on birchwood xylan producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains
physiological function
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Xyn10B is a trifunctional enzyme having endoxylanase, arabinofuranosidase and acetyl xylan esterase activities. Xyn10B is highly active on birchwood xylan producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains
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physiological function
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overexpression in Trichoderma reesei by fusing with xylanase Xyn2 from Trichoderma reesei as a carrier protein. The production of AXE in the transformant T2 is approximately 74% higher than that of the parent strain. The saccharification efficiency of rAXE gives approximately 23.2%, 22.7%, and 19.4% higher yield of reducing sugar in paddy straw, corn stover plus paddy straw mix (1:1 ratio), and corn stalk (delignified) hydrolysis
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physiological function
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sequence reveals a GH62 domain exhibiting alpha-L-arabinofuranosidase activity, in addition to the expected esterase domain
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physiological function
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expression in Arabidopsis thaliana. The protein is targeted to the apoplast by its native signal peptide, resulting in elevated acetyl esterase activity in soluble and wall-bound protein extracts and reduced xylan acetylation. No significant alterations in cell wall composition are observed. The xylans of transgenic lines are more easily digested by a beta-1,4-endoxylanase, and more readily extracted by hot water, acids or alkali. Transgenic plants develop normally and show increased resistance to the biotrophic pathogen Hyaloperonospora arabidopsidis
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physiological function
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wild-type is a trifunctional xylanolytic enzyme exhibiting alpha-L-arabinofuranosidase, endoxylanase, and acetylxylan esterase activities
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physiological function
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Xyn10B is a trifunctional enzyme having endoxylanase, arabinofuranosidase and acetyl xylan esterase activities. Xyn10B is highly active on birchwood xylan producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains
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physiological function
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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
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additional information
the active site of the enzyme is located at the base of a groove lined by two tryptophan residues, Trp158 and Trp195 are arranged in a parallel fashion on either side above the active site
additional information
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the active site of the enzyme is located at the base of a groove lined by two tryptophan residues, Trp158 and Trp195 are arranged in a parallel fashion on either side above the active site
additional information
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the active site of the enzyme is located at the base of a groove lined by two tryptophan residues, Trp158 and Trp195 are arranged in a parallel fashion on either side above the active site
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