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evolution
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phylogenetic DNA and amino acid sequence analysis of the Ascomycota family feruoyl esterases, comparisons and taxonomic classification, overview
evolution
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feruloyl esterases are a subclass of the carboxylic acid esterases, E.C. 3.1.1.1, that are able to hydrolyze the ester bond between hydroxycinnamic acids and sugars present in the plant cell walls
evolution
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the enzyme belongs to the fungal tannase family
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.1 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.11 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.12 belongs to the subfamily FEF 11A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.13 belongs to the subfamily FEF 12B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.2 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.3 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.4 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.5 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.6 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.7 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.8 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
Q2TWG0, Q2TX21, Q2TYH6, Q2U9N5, Q2UBD6, Q2UF27, Q2UH24, Q2UII1, Q2UMX6, Q2UNW5, Q2UP89, Q75P26 the isozyme A.O.9 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
evolution
the termite-derived isozymes form a distinct subclass of feroyl esterases
evolution
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the isozyme A.O.6 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.1 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.7 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.8 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.3 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.9 belongs to the subfamily FEF 7A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.12 belongs to the subfamily FEF 11A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.2 belongs to the subfamily FEF 4A of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.11 belongs to the subfamily FEF 4B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.4 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.13 belongs to the subfamily FEF 12B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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evolution
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the isozyme A.O.5 belongs to the subfamily FEF 6B of the ferouyl esterase family, structural similarities in the secondary structure elements of FEF subfamily members, structure modeling, overview
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malfunction
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when gene faeT is inactivated, the size of the esterase halo clearly decreased. When gene faeD is inactivated, only very low residual feruoyl esterase activity is detected, as observed in the faeD faeT double mutant
malfunction
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when gene faeT is inactivated, the size of the esterase halo clearly decreased. When gene faeD is inactivated, only very low residual feruoyl esterase activity is detected, as observed in the faeD faeT double mutant
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physiological function
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endpoint in vitro-dry-matter-digestibility is enhanced by FAEA expression in some individual plants. Initial rates of cell wall fermentation are enhanced under rumen conditions by FAEA expression
physiological function
FaeA is a type A enzyme
physiological function
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Xyn10D-Fae1A possesses both endo-beta-1,4-xylanase and ferulic acid esterase activities, Glu280 is an important residue for xylanase activity and Ser629 is an important residue for ferulic acid esterase activity. When incubated in combination with Xyn10D-Fae1A, the beta-D-glucosidase Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, thus these two enzymes function synergistically to depolymerize xylan. Two catalytic domains for Xyn10D-Fae1A are functionally coupled
physiological function
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the two feruloyl esterases, FaeD and FaeT, cleave the ester link between ferulate and the pectic or xylan chains. FaeD is an extracellular protein secreted by the Out system, responsible for pectinase secretion. Feruloyl esterases dissociate internal cross-links in the polysaccharide network of the plant cell wall, suppress the polysaccharide esterifications, and liberate ferulic acid, which contributes to the induction of pectate lyases. Together, these effects of feruloyl esterases could facilitate soft rot disease caused by pectinolytic bacteria. FaeD appears to be responsible for most feruloyl esterase activity in Dickeya dadantii
physiological function
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feruloyl esterase is a key bacterial enzyme involved in ferulate production from agricultural biomass
physiological function
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the enzyme activity can cause inhibition of cell growth due to production of toxic phenolic products, overview
physiological function
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coexpression of vacuole- or apoplast-targeted ferulic acid esterase from Aspergillus niger and senescence-induced and apoplast-targeted beta-1,4 endo-xylanase from Trichoderma reesei in Festuca arundinacea. Xylanase activity in senescent leaves increases and ferulic acid esterase activity decreases after tillering. Plants coexpressing both enzymes in the apoplast, with the lowest levels of ferulate monomers and dimers and the lowest levels of cell wall arabinoxylans, release ten times more cell wall hydroxycinnamic acids and five times more arabinoxylan from the cell wall on autodigestion compared to expression of ferulic acid esterase or xylanase alone. These plants also show a 31% increase in cellulase-mediated release of reducing sugars, a 5% point increase in in vitro dry matter digestibility and a 23% increase in acetyl bromide-soluble lignin. Plant growth is adversely affected by expressing ferulic acid esterase in the apoplast, giving plants with narrower shorted leaves, and a 71% decrease in biomass
physiological function
expression in Medicago sativa and Nicotiana tabacum using different signaling peptides to target type B ferulic acid esterase proteins to the apoplast, chloroplast, endoplasmic reticulum and vacuole. In Nicotiana leaves, the protein accumulates at high levels in all target sites, except chloroplast. Stable transformed lines of alfalfa possess modified cell wall morphology and composition with a reduction in ester linkages and elevated lignin content. These are more recalcitrant to digestion by mixed ruminal microorganisms. Delignification by alkaline peroxide treatment followed by exposure to a commercial cellulase mixture results in higher glucose release from transgenic lines as compared to the control line
physiological function
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feruloyl esterase production is associated with phylogenetic clades 4, 11, and particularly clade 8. Clade 8 strains NRRL 58552 and NRRL 62041 produces the highest levels of feruloyl esterase among strains tested
physiological function
non-embryogenic cell suspension cultures of Festuca arundinacea expressing Aspergillus niger faeA targeted to the apoplast, or endoplasmic reticulum, or to the vacuole, show both reduced ferulate levels and increased levels of xylanase-mediated release of wall phenolics on autodigestion as well as increased rates of cell wall digestion in a simulated rumen environment
physiological function
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Xyn10D-Fae1A possesses both endo-beta-1,4-xylanase and ferulic acid esterase activities, Glu280 is an important residue for xylanase activity and Ser629 is an important residue for ferulic acid esterase activity. When incubated in combination with Xyn10D-Fae1A, the beta-D-glucosidase Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, thus these two enzymes function synergistically to depolymerize xylan. Two catalytic domains for Xyn10D-Fae1A are functionally coupled
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physiological function
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the enzyme activity can cause inhibition of cell growth due to production of toxic phenolic products, overview
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physiological function
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the enzyme activity can cause inhibition of cell growth due to production of toxic phenolic products, overview
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physiological function
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the two feruloyl esterases, FaeD and FaeT, cleave the ester link between ferulate and the pectic or xylan chains. FaeD is an extracellular protein secreted by the Out system, responsible for pectinase secretion. Feruloyl esterases dissociate internal cross-links in the polysaccharide network of the plant cell wall, suppress the polysaccharide esterifications, and liberate ferulic acid, which contributes to the induction of pectate lyases. Together, these effects of feruloyl esterases could facilitate soft rot disease caused by pectinolytic bacteria. FaeD appears to be responsible for most feruloyl esterase activity in Dickeya dadantii
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additional information
EstF27 contains one conserved active site of pentapeptide motif G-X-S-XG, amino acid positions from 149 to 153, and a putative catalytic triad comprising His73, Asp123 and Ser151 in the G-X-S-X-G
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
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active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
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active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
additional information
homology-based modelling, overview
additional information
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homology-based modelling, overview
additional information
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the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
the catalytic triad is formed by Ser121, Asp215 and His244
additional information
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the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
the catalytic triad is formed by Ser123, Asp212 and His241
additional information
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the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
the catalytic triad is formed by Ser124, Asp215 and His244
additional information
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the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
the catalytic triad is formed by Ser125, Asp216 and His245
additional information
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the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
the catalytic triad is formed by Ser126, Asp215 and His244
additional information
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the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
the catalytic triad is formed by Ser128, Asp215 and His244
additional information
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the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad is formed by Ser131, Asp222 and His251
additional information
the catalytic triad of Ser-Glu-His is unique among feruloyl esterases, the enzyme has a G-X-S-X-G motif
additional information
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the catalytic triad of Ser-Glu-His is unique among feruloyl esterases, the enzyme has a G-X-S-X-G motif
additional information
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the enzyme shows a synergistic interaction with the Aspergillus usamii GH family 11 xylanase A. Three-dimensional structure determination, modeling, overview. The enzyme has a globular shape with a catalytic triad Ser133-Asp194-His247, and is composed mainly of one major nine-stranded beta-sheet, two minor two-stranded beta-sheets, and seven alpha-helices, core topology is alpha/beta-hydrolase fold
additional information
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the enzyme structure consists of a catalytic alpha/beta-hydrolase fold domain and a large lid domain with a unique fold, binding models of substrates and docking analysis, overview. The catalytic triad of the enzyme comprises residues Ser203, Asp417, and His457, and the serine and histidine residues are directly connected by a disulfide bond of the neighboring cysteine residues, Cys202 and Cys458. The CS-D-HC structural motif plays an essential role in the function of the active site
additional information
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the enzyme shows a synergistic interaction with the Aspergillus usamii GH family 11 xylanase A. Three-dimensional structure determination, modeling, overview. The enzyme has a globular shape with a catalytic triad Ser133-Asp194-His247, and is composed mainly of one major nine-stranded beta-sheet, two minor two-stranded beta-sheets, and seven alpha-helices, core topology is alpha/beta-hydrolase fold
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additional information
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homology-based modelling, overview
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additional information
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active site residues of isozyme A.O.8 are Ser177, Asp401, and His437
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additional information
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active site residues of isozyme A.O.2 are Ser183, Asp419 and His465
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