3.2.1.136: glucuronoarabinoxylan endo-1,4-beta-xylanase
This is an abbreviated version!
For detailed information about glucuronoarabinoxylan endo-1,4-beta-xylanase, go to the full flat file.
Word Map on EC 3.2.1.136
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3.2.1.136
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xylans
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glucuronoxylans
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xylanases
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xylooligosaccharides
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arabinoxylans
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beechwood
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meglca
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thermobacillus
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4-o-methyl-d-glucuronic
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xylobiohydrolase
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aldouronic
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xylopyranosyl
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glucuronoarabinoxylans
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xylotetraose
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xylotriose
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xylanilyticus
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4-o-methylglucuronate
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biofuel production
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barcinonensis
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arabinofuranosidase
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arabinofuranohydrolase
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methylglucuronoxylans
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cellulolyticus
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food industry
- 3.2.1.136
- xylans
- glucuronoxylans
- xylanases
- xylooligosaccharides
- arabinoxylans
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beechwood
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meglca
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thermobacillus
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4-o-methyl-d-glucuronic
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xylobiohydrolase
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aldouronic
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xylopyranosyl
- glucuronoarabinoxylans
- xylotetraose
- xylotriose
- xylanilyticus
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4-o-methylglucuronate
- biofuel production
- barcinonensis
- arabinofuranosidase
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arabinofuranohydrolase
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methylglucuronoxylans
- cellulolyticus
- food industry
Reaction
Synonyms
1,4-beta-D-xylan xylanohydrolase, Agu115A, beta-1,4-endoxylanase, bifunctional cellulase/xylanase, endo-beta-xylanase, endoarabinoxylanase, endoglucanase, endoxylanase, feraxan endoxylanase, feraxanase, GH11 endoxylanase, GH115 alpha-glucuronidase, GH30 endoxylanase C, GH30 xylanase, glucuronoxylan xylanohydrolase, glucuronoxylan xylohydrolase, glucuronoxylan-specific xylanase A, glucuronoxylan-specific Xyn30D, glucuronoxylanase, glucuronoxylanase GH30, GuXN 30, M2, M4, TLX, Tx-Xyl, xylanase 30 A, xylanase C, xylanase, glucuronoarabinoxylan endo-1,4-beta-, Xyn30A, Xyn30D, XynA, XynC, XynGH30
ECTree
3.2.1.136 glucuronoarabinoxylan endo-1,4-beta-xylanaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.136 - glucuronoarabinoxylan endo-1,4-beta-xylanase
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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-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O
?
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-
-
?
4-O-methyl-beta-D-glucuronopyranosyl-1,2-(beta-1,4-xylan) + H2O
4-O-methyl-beta-D-glucopyranuronosyl-(1-2)-[beta-D-xylopyranosyl-(1-4)]-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + ?
-
-
-
-
?
4-O-methyl-D-glucoxylan + H2O
?
elimination of the carboxyl groups of substrate leads to more than 300fold reduction of specific activity
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-
?
4-O-methyl-D-glucuronoxylan + H2O
4-methyl-D-glucuronate + xylan
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-
-
-
?
arabinoxylan + H2O
reduced sugars
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azurine-cross-linked arabinoxylan
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-
?
beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + h2O
?
-
-
-
?
glucuronoarabinoxylan-lignin + H2O
reduced xylose + ?
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four types of in vitro reconstituted non-covalent glucuronoarabinoxylan-model lignin nanocomposites, each displaying different lignin contents, are synthesized as enzyme substrates, method overview. The nanocomposites contain a mixture of free glucuronoarabinoxylan chains with non-covalent glucuronoarabinoxylan-lignin complexes, morphology and size distribution analysis. Increased particle size is directly related to the solubility and reactivity of coniferyl alcohol, as reflected by changes in the amount of beta-O-4 linkages. Negative correlation between the proportion and organization patterns of lignin dehydrogenation polymer in the nanocomposites and enzyme activity, kinetic analysis
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-
?
maize xylan + H2O
?
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i.e. heteroxylan with glucuronic acid side chain, enzyme recognizes glucuronic acid side chains along the xylan main chain and mediates hydrolysis of beta-1,4-xylosyl linkages of adjacent unsubstituted xylosyl residues, endo-type hydrolase, possible recognition sites
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-
?
Remazol brilliant blue-carboxymethylcellulose + H2O
glucose + cellobiose + cellotriose + cellotetraose + high-molecular-mass oligosaccharides
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cellulose activity
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?
rye glucuronoarabinoxylan + H2O
?
the enzyme shows calcium-dependent glucuronic acid binding and also some binding to arabinose in presence of calcium chelating EDTA. Recognition of uronic acid by the CBM35 domains is always dependent on calcium, which interacts with the carboxylate of the ligand. Glu129, from the loop linking beta10-beta11, is a determinant of substrate specificity
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-
?
Vigna angularis xylan + H2O
?
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i.e. heteroxylan with glucuronic acid side chain
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-
?
xylan + H2O
xylose + arabinose + xylobiose + high-molecular-mass oligosaccharides
xylan from birchwood
xylanase activity
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?
4-O-methyl-D-glucuronoxylan + H2O
?
esterification of substrate leads to more than 300fold reduction of specific activity
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-
?
4-O-methylglucuronoxylan + H2O
?
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the limit product is an aldouronate substituted with a single 4-O-methylglucuronate moiety penultimate to the reducing terminus
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?
4-O-methylglucuronoxylan + H2O
?
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the limit product is an aldouronate substituted with a single 4-O-methylglucuronate moiety penultimate to the reducing terminus
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?
arabinoxylan + H2O
reducing sugars
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39% arabinan, 62% xylan from wheat, substrate water activity range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
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?
arabinoxylan + H2O
reducing sugars
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39% arabinan, 62% xylan from wheat, substrate water activity range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
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?
arabinoxylan + H2O
reducing sugars
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39% arabinan, 62% xylan from wheat, substrate water activity range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
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?
eucalyptus wood powder + H2O
?
the enzyme releases from eucalyptus wood powder acidic oligosaccharides of the formula MeGlcAXylnAcn-1, MeGlcAXylnAcn-2, MeGlcAXylnAcn-3 for n =5-8, and aldouronic acids of the formula MeGlcAXylnAcn-1 and MeGlcAXylnAcn-2 for n = 3-4
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-
?
eucalyptus wood powder + H2O
?
the enzyme releases from eucalyptus wood powder acidic oligosaccharides of the formula MeGlcAXylnAcn-1, MeGlcAXylnAcn-2, MeGlcAXylnAcn-3 for n =5-8, and aldouronic acids of the formula MeGlcAXylnAcn-1 and MeGlcAXylnAcn-2 for n = 3-4
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-
?
feraxan + H2O
?
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i.e. feruloylated glucuronoarabinoxylans, highly specific endo-type hydrolase
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?
feraxan + H2O
?
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hydrolyzes feraxan both in intact maize coleophile cell wall and maize arabinoxylans extracted from cell walls with alkaline
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?
feraxan + H2O
?
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selectively dissociates feraxan from maize cell wall
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-
?
glucuronoarabinoxylan + H2O
?
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the enzyme hydrolyzes glucuronoarabinoxylan to release a series of aldouronic acid mixtures with a methylglucuronic acid branch
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-
?
glucuronoarabinoxylan + H2O
?
Paenibacillus amylolyticus KCTC 3005
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the enzyme hydrolyzes glucuronoarabinoxylan to release a series of aldouronic acid mixtures with a methylglucuronic acid branch
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-
?
glucuronoxylan + H2O
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the cleavage of the glucuronoxylan main chain takes place exclusively at the second glycosidic linkage from the branch towards the reducing end of the polysaccharide chain
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?
lignocellulose + H2O
reducing sugars
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aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
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?
lignocellulose + H2O
reducing sugars
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aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
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?
lignocellulose + H2O
reducing sugars
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aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
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?
additional information
?
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enzyme also acts on xylans, reaction of EC 3.2.1.8
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?
additional information
?
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isoform XynGH30 has high binding affinity with different xylans through an exothermic mechanism, with relatively higher affinity against arabinoxylans. The enzyme shows negligible affinity towards celluloses, pectins and other polysaccharides but predominantly interacts with ligands containing a xylan backbone (beta-1,4-xylopyranose)
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-
?
additional information
?
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isoform XynGH30 has high binding affinity with different xylans through an exothermic mechanism, with relatively higher affinity against arabinoxylans. The enzyme shows negligible affinity towards celluloses, pectins and other polysaccharides but predominantly interacts with ligands containing a xylan backbone (beta-1,4-xylopyranose)
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-
?
additional information
?
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no activity on arabinoxylans and tamarind xyloglucan
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-
?
additional information
?
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Acetivibrio thermocellus DSM 1237
isoform XynGH30 has high binding affinity with different xylans through an exothermic mechanism, with relatively higher affinity against arabinoxylans. The enzyme shows negligible affinity towards celluloses, pectins and other polysaccharides but predominantly interacts with ligands containing a xylan backbone (beta-1,4-xylopyranose)
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-
?
additional information
?
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Acetivibrio thermocellus DSM 1237
enzyme also acts on xylans, reaction of EC 3.2.1.8
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-
?
additional information
?
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the enzyme recognizes glucuronic acid side chains along the xylan main chain and mediates the hydrolysis of the beta-1,4-xylosyl linkages of the adjacent unsubstituted xylosyl residues
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-
?
additional information
?
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the enzyme requires the recognition of glucuronic acid side chains for hydrolysis and shows no activity on linear xylooligosaccharides
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?
additional information
?
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the enzyme requires the recognition of glucuronic acid side chains for hydrolysis and shows no activity on linear xylooligosaccharides
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?
additional information
additional information
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not: cellulose, carboxymethyl cellulose, lichenan, oat or barley beta-glucan, laminarin, dextran, starch, citrus or maize pectin, polyuronides, arabinan, galactan, arabinogalactan, yeast mannan, galactomannan
no products are mono-, di-, tri-, or tetramers of xylose and/or arabinose
?
additional information
additional information
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not: cellulose, carboxymethyl cellulose, lichenan, oat or barley beta-glucan, laminarin, dextran, starch, citrus or maize pectin, polyuronides, arabinan, galactan, arabinogalactan, yeast mannan, galactomannan
products from hydrolysis of extracted maize arabinoxylan: major linkages in smaller fractions are terminal arabinofuranosyl, 5-linked arabinofuranosyl, 4-linked xylopyranoslyl, 3,4-linked xylopyranosyl and terminal glucuronosyl residues
?
additional information
additional information
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not: larch arabino-1,4-beta-D-xylan, Rhodymenia 1,3-1,4-beta-D-xylan
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-
?
additional information
additional information
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not: larch arabino-1,4-beta-D-xylan, Rhodymenia 1,3-1,4-beta-D-xylan
no products are mono-, di-, tri-, or tetramers of xylose and/or arabinose
?
additional information
additional information
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not: larch arabino-1,4-beta-D-xylan, Rhodymenia 1,3-1,4-beta-D-xylan
products from hydrolysis of extracted maize arabinoxylan: major linkages in smaller fractions are terminal arabinofuranosyl, 5-linked arabinofuranosyl, 4-linked xylopyranoslyl, 3,4-linked xylopyranosyl and terminal glucuronosyl residues
?
additional information
additional information
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no substrates are xylan derivatives whose glucuronic acid residues have been converted to glucose, beta-1,4-xylan
no products are xylohomooligomers
?
additional information
additional information
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no substrates are xylan derivatives whose glucuronic acid residues have been converted to glucose, beta-1,4-xylan
structural analysis of products of maize xylan: sugar composition and glycosidic linkage composition of xylan fragments
?
additional information
additional information
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the enzyme releases mainly xylose and xylobiose from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methyl-D-glucuronoxylan and rhodymenan, the enzyme releases an acidic xylooligosaccharide from 4-O-methyl-D-glucoronoxylan, and an isomeric xylotetraose and anisomeric xylopentaose from rhodymenan, enzyme hydrolyses [1-3H]-xylooligosaccharides
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?
