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4-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O
?
-
-
-
?
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
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
4-methyl-D-glucuronate + xylan
-
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
?
4-O-methylglucoxylan + H2O
?
-
-
-
-
?
4-O-methylglucuronoxylan + H2O
?
arabinoxylan + H2O
reduced sugars
-
azurine-cross-linked arabinoxylan
-
-
?
arabinoxylan + H2O
reducing sugars
beechwood glucuronoxylan + H2O
?
-
highest activity
-
-
?
beet debranched arabinan + H2O
?
-
-
-
-
?
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
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
carob galactomannan + H2O
?
-
-
-
-
?
eucalyptus wood powder + H2O
?
glucuronoarabinoxylan + H2O
?
glucuronoarabinoxylan + H2O
reduced xylose + ?
-
-
-
-
?
glucuronoarabinoxylan-lignin + H2O
reduced xylose + ?
-
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
-
-
?
konjac glucomannan + H2O
?
-
-
-
-
?
larch wood arabinoglalctan + H2O
?
-
-
-
-
?
lignocellulose + H2O
reducing sugars
maize xylan + H2O
?
-
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
-
-
?
methylglucuronoxylotetraose + H2O
?
-
maximal activity
-
-
?
Remazol brilliant blue-carboxymethylcellulose + H2O
glucose + cellobiose + cellotriose + cellotetraose + high-molecular-mass oligosaccharides
-
cellulose activity
-
?
rye arabinoxylan + H2O
?
-
-
-
?
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
-
-
?
Vigna angularis xylan + H2O
?
-
i.e. heteroxylan with glucuronic acid side chain
-
-
?
wheat arabinoxylan + H2O
?
xylan + H2O
xylose + arabinose + xylobiose + high-molecular-mass oligosaccharides
xylan from birchwood
xylanase activity
-
?
additional information
?
-
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
esterification of substrate leads to more than 300fold reduction of specific activity
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
special substrate
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
?
-
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
?
-
-
-
?
4-O-methylglucuronoxylan + H2O
?
-
-
-
?
4-O-methylglucuronoxylan + H2O
?
-
the limit product is an aldouronate substituted with a single 4-O-methylglucuronate moiety penultimate to the reducing terminus
-
?
4-O-methylglucuronoxylan + H2O
?
-
the limit product is an aldouronate substituted with a single 4-O-methylglucuronate moiety penultimate to the reducing terminus
-
?
arabinoxylan + H2O
reducing sugars
-
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
-
?
arabinoxylan + H2O
reducing sugars
-
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
-
?
arabinoxylan + H2O
reducing sugars
-
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
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
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
-
-
?
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
-
-
?
feraxan + H2O
?
-
i.e. feruloylated glucuronoarabinoxylans, highly specific endo-type hydrolase
-
-
?
feraxan + H2O
?
-
hydrolyzes feraxan both in intact maize coleophile cell wall and maize arabinoxylans extracted from cell walls with alkaline
-
-
?
feraxan + H2O
?
-
selectively dissociates feraxan from maize cell wall
-
-
?
glucuronoarabinoxylan + H2O
?
-
the enzyme hydrolyzes glucuronoarabinoxylan to release a series of aldouronic acid mixtures with a methylglucuronic acid branch
-
-
?
glucuronoarabinoxylan + H2O
?
-
the enzyme hydrolyzes glucuronoarabinoxylan to release a series of aldouronic acid mixtures with a methylglucuronic acid branch
-
-
?
glucuronoxylan + H2O
?
-
-
-
?
glucuronoxylan + H2O
?
-
-
-
?
glucuronoxylan + H2O
?
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
-
-
?
glucuronoxylan + H2O
?
-
-
-
-
?
glucuronoxylan + H2O
?
-
-
-
-
?
lignocellulose + H2O
reducing sugars
-
aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
-
?
lignocellulose + H2O
reducing sugars
-
aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
-
?
lignocellulose + H2O
reducing sugars
-
aim for fuel production are natural substrates such as corn stover, switchgrass, wheat straw
oligosaccharides, xylobiose, xylotriose
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
additional information
?
-
enzyme also acts on xylans, reaction of EC 3.2.1.8
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
-
no activity on arabinoxylans and tamarind xyloglucan
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
enzyme also acts on xylans, reaction of EC 3.2.1.8
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme requires the recognition of glucuronic acid side chains for hydrolysis and shows no activity on linear xylooligosaccharides
-
-
?
additional information
?
-
-
the enzyme requires the recognition of glucuronic acid side chains for hydrolysis and shows no activity on linear xylooligosaccharides
-
-
?
additional information
additional information
-
-
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
-
-
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
-
-
not: larch arabino-1,4-beta-D-xylan, Rhodymenia 1,3-1,4-beta-D-xylan
-
-
?
additional information
additional information
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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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Nishitani, K.; Nevins, D.J.
Enzymic analysis of feruloylated arabinoxylans (Feraxan) derived from Zea mays cell walls. I. Purification of novel enzymes capable of dissociating Feraxan fragments from Zea mays coleoptile cell wall
Plant Physiol.
87
883-890
1988
Bacillus subtilis
brenda
Nishitani, K.; Nevins, D.J.
Glucuronoxylan xylanohydrolase. A unique xylanase with the requirement for appendant glucuronosyl units
J. Biol. Chem.
266
6539-6543
1991
Bacillus subtilis
brenda
Nevins, D.J.; Nishitani, K.
Purification and characterization of Bacillus feraxanase, a highly specific enzyme for hydrolysis of complex polysaccharides, WO9001059 A1
PCT Int. Appl.
1990
1-35
1990
Bacillus subtilis
-
brenda
Bennett, N.A.; Ryan, J.; Biely, P.; Vrsanska, M.; Kremnicky, L.; Macris, B.J.; Kekos, D.; Christakopoulos, P.; Katapodis, P.; Claeyssens, M.; Nerinckx, W.; Ntauma, P.; Bhat, M.K.
Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882
Carbohydr. Res.
306
445-455
1998
Thermomyces lanuginosus
brenda
Dornez, E.; Cuyvers, S.; Gebruers, K.; Delcour, J.A.; Courtin, C.M.
Contribution of wheat endogenous and wheat kernel associated microbial endoxylanases to changes in the arabinoxylan population during breadmaking
J. Agric. Food Chem.
56
2246-2253
2008
Triticum aestivum
brenda
St John, F.J.; Rice, J.D.; Preston, J.F.
Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan
J. Bacteriol.
188
8617-8626
2006
Bacillus subtilis
brenda
Smith, W.A.; Thompson, D.N.; Thompson, V.S.; Radtke, C.W.; Carter, B.
Assessment of xylanase activity in dry storage as a potential method of reducing feedstock cost
Appl. Biochem. Biotechnol.
154
108-122
2009
Aspergillus niger, Thermomyces lanuginosus, Trichoderma longibrachiatum
brenda
Perez-Avalos, O.; Sanchez-Herrera, L.M.; Salgado, L.M.; Ponce-Noyola, T.
A bifunctional endoglucanase/endoxylanase from Cellulomonas flavigena with potential use in industrial processes at different pH
Curr. Microbiol.
57
39-44
2008
Cellulomonas flavigena (A1XM14), Cellulomonas flavigena CDBB-531 (A1XM14)
brenda
St. John, F.J.; Godwin, D.K.; Preston, J.F.; Pozharski, E.; Hurlbert, J.C.
Crystallization and crystallographic analysis of Bacillus subtilis xylanase C
Acta Crystallogr. Sect. F
65
499-503
2009
Bacillus subtilis (Q45070)
brenda
Urbanikova, L.; Vrsanska, M.; Morkeberg Krogh, K.B.; Hoff, T.; Biely, P.
Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase
FEBS J.
278
2105-2116
2011
Dickeya chrysanthemi (Q46961)
brenda
St John, F.J.; Hurlbert, J.C.; Rice, J.D.; Preston, J.F.; Pozharski, E.
Ligand bound structures of a glycosyl hydrolase family 30 glucuronoxylan xylanohydrolase
J. Mol. Biol.
407
92-109
2011
Bacillus subtilis subsp. subtilis (Q45070), Bacillus subtilis subsp. subtilis 168 (Q45070)
brenda
Boukari, I.; Remond, C.; ODonohue, M.; Chabbert, B.
Effect of lignin content on a GH11 endoxylanase acting on glucuronoarabinoxylan-lignin nanocomposites
Carbohydr. Polym.
89
423-431
2012
Thermobacillus xylanilyticus
brenda
Sainz-Polo, M.A.; Valenzuela, S.V.; Gonzalez, B.; Pastor, F.I.; Sanz-Aparicio, J.
Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity
J. Biol. Chem.
289
31088-31101
2014
Paenibacillus barcinonensis (H6WCZ0)
brenda
Freire, F.; Verma, A.; Bule, P.; Alves, V.; Fontes, C.; Goyal, A.; Najmudin, S.
Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum
Acta Crystallogr. Sect. D
72
1162-1173
2016
Acetivibrio thermocellus (A3DJS9), Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237 (A3DJS9)
brenda
Biely, P.; Malovikova, A.; Hirsch, J.; Morkeberg Krogh, K.B.; Ebringerova, A.
The role of the glucuronoxylan carboxyl groups in the action of endoxylanases of three glycoside hydrolase families: A study with two substrate mutants
Biochim. Biophys. Acta
1850
2246-2255
2015
Dickeya chrysanthemi (Q46961), Dickeya chrysanthemi
brenda
Verma, A.; Goyal, A.
A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans
J. Mol. Catal. B
129
6-14
2016
Acetivibrio thermocellus (A3DJS9), Acetivibrio thermocellus DSM 1237 (A3DJS9)
-
brenda
Maehara, T.; Yagi, H.; Sato, T.; Ohnishi-Kameyama, M.; Fujimoto, Z.; Kamino, K.; Kitamura, Y.; St John, F.; Yaoi, K.; Kaneko, S.
GH30 glucuronoxylan-specific xylanase from Streptomyces turgidiscabies C56
Appl. Environ. Microbiol.
84
e01850-17
2018
Streptomyces turgidiscabies, Streptomyces turgidiscabies C56
brenda
Rhee, M.S.; Sawhney, N.; Kim, Y.S.; Rhee, H.J.; Hurlbert, J.C.; St John, F.J.; Nong, G.; Rice, J.D.; Preston, J.F.
GH115 alpha-glucuronidase and GH11 xylanase from Paenibacillus sp. JDR-2 potential roles in processing glucuronoxylans
Appl. Microbiol. Biotechnol.
101
1465-1476
2017
Paenibacillus sp. JDR-2
brenda
Puchart, V.; Fra?ova, L.; M?rkeberg Krogh, K.B.R.; Hoff, T.; Biely, P.
Action of different types of endoxylanases on eucalyptus xylan in situ
Appl. Microbiol. Biotechnol.
102
1725-1736
2018
Bacillus subtilis (Q45070), Bacillus subtilis 168 (Q45070)
brenda
Suchova, K.; Kozmon, S.; Puchart, V.; Malovikova, A.; Hoff, T.; Morkeberg Krogh, K.B.R.; Biely, P.
Glucuronoxylan recognition by GH 30 xylanases A study with enzyme and substrate variants
Arch. Biochem. Biophys.
643
42-49
2018
Dickeya chrysanthemi
brenda
St John, F.; Crooks, C.; Dietrich, D.; Hurlbert, J.
Xylanase 30 A from Clostridium thermocellum functions as a glucuronoxylan xylanohydrolase
J. Mol. Catal. B
133
S445-S451
2016
Acetivibrio thermocellus
-
brenda
Nam, g.; Jang, M.; Kim, M.; Lee, J.; Lee, M.; Kim, T.
Enzymatic characterization of Paenibacillus amylolyticus xylanases GH10 and GH30 for xylan hydrolysis
Korean J. Microbiol.
52
463-472
2016
Paenibacillus amylolyticus, Paenibacillus amylolyticus KCTC 3005
-
brenda