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alpha-L-arabinofuranosidase-treated root arabinogalactan proteins from radish + H2O
?
relative activity: 9.3
-
-
?
beta-(1,3)-D-galactooligosaccharides + H2O
D-galactose + ?
beta-(1,3)-galactobiose + H2O
D-galactose
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
beta-(1-3)-galactobiose + H2O
D-galactose
beta-(1-6)-galactopentaose + H2O
beta-(1-6)-D-galactotetraose + D-galactose
50% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-(1-6)-galactotetraose + H2O
beta-(1-6)-D-galactotriose + D-galactose
68% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-(1-6)-galactotriose + H2O
beta-(1-6)-D-galactobiose + D-galactose
49% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-1,3-beta-1,6-galactan + H2O
?
relative activity: 3.1%
-
-
?
beta-1,3-D-galactobiose + H2O
2 D-galactose
beta-1,3-D-galactobiose + H2O
D-galactose
beta-1,3-D-galactopentaose + H2O
D-galactose + ?
beta-1,3-D-galactotetraose + H2O
D-galactose + ?
beta-1,3-D-galactotriose + H2O
D-galactose + ?
-
-
-
?
beta-1,3-galactan + H2O
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
beta-1,3-galactotriose + H2O
D-galactose + beta-(1,3)-galactobiose
beta-1,6-Gal2-galactitol + H2O
beta-1,6-Gal2 + galactitol
the enzyme specifically releases beta-1,6-Gal2 but not galactose from beta-1,6-Gal2-Gat
-
-
?
beta-1,6-Gal3 + H2O
beta-1,6-Gal2 + D-galactose
-
-
-
?
beta-1,6-galactooligosaccharides + H2O
beta-1,6-Gal2 + ?
the enzyme releases beta-1,6-Gal2 from beta-1,6-galactooligosaccharides (beta-1,6-Gal>9) in a time-dependent manner with low rates of beta-1,6-Gal3 and beta-1,6-Gal4
-
-
?
beta-D-Gal-[(1->3)-beta-D-Gal]n + H2O
beta-D-Gal-[(1->3)-beta-D-Gal]n-1 + D-galactose
-
only beta-(1, 3) oligomers act as substrates
-
?
beta-galactosido-(1-3)-beta-galactosido-(1-6)-galactoside + H2O
beta-galactosido-(1-3)-beta-galactoside + D-galactose
42% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-galactosido-(1-6)-beta-galactosido-(1-3)-galactoside + H2O
beta-galactosido-(1-6)-beta-galactoside + D-galactose
40% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
dearabinosylated gum arabic + H2O
?
dearabinosylated larch wood arabinogalactan + H2O
?
best substrate
-
-
?
dyed de-arabinosylated gum arabic + H2O
?
-
preparation of de-arabinosylated arabinogalactan-(protein)s as substrates for determination of beta-galactanase activity, method development, covalent coupling of the RB5 dye to the substrate, overview
-
-
?
larch type II arabinogalactan + H2O
?
degradation profiles of type II AG
-
-
?
larch type II arabinogalactan + H2O
beta-1,6-Gal2 + ?
release of galactobiose, beta-1,6-Gal2, degradation profiles of type II AG
-
-
?
larch wood arabinogalactan + H2O
?
larch wood arabinogalactan + H2O
D-galactose + beta-(1->6)-D-galactobiose + beta-(1->6)-D-galactotriose + O-alpha-L-arabinofuranosyl-(1->3)-O-beta-D-galactopyranosyl-(1->6)-O-beta-D-galactopyranosyl-(1->6)-D-galactopyranose + O-beta-D-galactopyranosyl-(1->6)-[O-alpha-L-arabinofuranosyl-(1->3)-]-O-beta-D-galactopyranosyl-(1->6)-D-galactopyranose + ?
-
the enzyme bypasses the branching points of beta-1,3-galactan backbones in larch wood arabinogalactan
-
-
?
methyl-beta-1,3-D-galactopentaoside + H2O
methyl-beta-1,3-D-galactotetraoside + D-galactose
methyl-beta-1,3-D-galactotetraoside + H2O
methyl-beta-1,3-D-galactotrioside + D-galactose
p-nitrophenyl-beta-galactoside + H2O
p-nitrophenol + beta-galactose
-
-
-
?
sugar beet debranched L-arabinan + H2O
?
-
-
-
?
type II arabinogalactan + H2O
?
-
-
-
?
additional information
?
-
beta-(1,3)-D-galactooligosaccharides + H2O
D-galactose + ?
-
-
-
-
?
beta-(1,3)-D-galactooligosaccharides + H2O
D-galactose + ?
-
-
-
-
?
beta-(1,3)-galactobiose + H2O
D-galactose
-
-
-
-
?
beta-(1,3)-galactobiose + H2O
D-galactose
-
-
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
-
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
8% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
-
the enzyme releases approximately 60% of the total D-galactose in the substrate
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
-
the enzyme releases approximately 60% of the total D-galactose in the substrate
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
-
relative activity: 100%. The enzyme hydrolizes only beta-1,3-linkage of two D-galactosyl residues at non-reducing ends of the substrate
-
-
?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
-
relative activity: 100%. The enzyme hydrolizes only beta-1,3-linkage of two D-galactosyl residues at non-reducing ends of the substrate
-
-
?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
relative activity: 119%. Enzyme hydrolyzes beta-1,3-linked galacto-oligosaccharides but does not hydrolyze beta-1,4-linked and beta-1,6-linked galacto-oligosaccharide. Ct1,3Gal43A also can not hydrolyze the beta-1,3-galactosyl linkage of beta-1,3-galactosyl galactosaminide, beta-1,3-galactosyl glucosaminide, or beta-1,3-galactosyl L-arabinofuranoside
-
-
?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
-
-
-
-
?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
44% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
-
relative activity: 57%
-
-
?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
-
relative activity: 57%
-
-
?
beta-(1-3)-galactobiose + H2O
D-galactose
relative activity: 31%
-
-
?
beta-(1-3)-galactobiose + H2O
D-galactose
-
-
-
?
beta-(1-3)-galactobiose + H2O
D-galactose
32% of the activity with p-nitrophenyl-beta-galactoside
-
-
?
beta-(1-3)-galactobiose + H2O
D-galactose
-
relative activity: 7.6%
-
-
?
beta-(1-3)-galactobiose + H2O
D-galactose
-
relative activity: 7.6%
-
-
?
beta-1,3-D-galactobiose + H2O
2 D-galactose
best beta-1,3-galactan substrate
-
-
?
beta-1,3-D-galactobiose + H2O
2 D-galactose
best beta-1,3-galactan substrate
-
-
?
beta-1,3-D-galactobiose + H2O
D-galactose
-
-
-
?
beta-1,3-D-galactobiose + H2O
D-galactose
-
-
-
?
beta-1,3-D-galactopentaose + H2O
D-galactose + ?
-
-
-
?
beta-1,3-D-galactopentaose + H2O
D-galactose + ?
-
-
-
?
beta-1,3-D-galactotetraose + H2O
D-galactose + ?
-
-
-
?
beta-1,3-D-galactotetraose + H2O
D-galactose + ?
-
-
-
?
beta-1,3-galactan + H2O
?
-
best substrate, mode of action, overview
-
-
?
beta-1,3-galactan + H2O
?
-
best substrate, mode of action, overview
-
-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
relative activity: 100%. Enzyme catalyzes hydrolysis only of beta-1,3-linked galactosyl oligosaccharides and polysaccharides. Enzyme does not hydrolyze beta-1,4-linked galactose-containing polysaccharides, such as pectic galactan and alpha-L-arabinofuranosidase-treated pectic galactan from lupine, and also does not hydrolyze laminarin, CM-curdlan, or beta-1,3-xylan, suggesting that the enzyme acts only on a beta-1,3-linked galactan chain
-
-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
preferred substrate
-
-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
preferred substrate
-
-
?
beta-1,3-galactotriose + H2O
D-galactose + beta-(1,3)-galactobiose
-
-
-
-
?
beta-1,3-galactotriose + H2O
D-galactose + beta-(1,3)-galactobiose
-
-
-
-
?
dearabinosylated gum arabic + H2O
?
-
-
-
?
dearabinosylated gum arabic + H2O
?
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
-
-
?
dearabinosylated gum arabic + H2O
?
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
-
-
?
dearabinosylated gum arabic + H2O
?
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
-
-
?
dearabinosylated gum arabic + H2O
?
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
-
-
?
gum arabic + H2O
?
-
-
-
?
gum arabic + H2O
?
-
-
-
?
gum arabic + H2O
?
-
-
-
?
gum arabic + H2O
?
-
-
-
?
gum arabic + H2O
?
-
weak substrate
-
-
?
larch wood arabinogalactan + H2O
?
-
-
-
?
larch wood arabinogalactan + H2O
?
the enzyme releases galactose, beta-1,6-D-galactobiose, beta-1,6-D-galactotriose, and beta-1,6-D-galactotriose substituted with a single arabinofuranose residue accompanied with unidentified oligosaccharides, indicating that the enzyme can by-pass the branching points of beta-1,3-galactan backbones
-
-
?
larch wood arabinogalactan + H2O
?
the enzyme releases galactose, beta-1,6-D-galactobiose, beta-1,6-D-galactotriose, and beta-1,6-D-galactotriose substituted with a single arabinofuranose residue accompanied with unidentified oligosaccharides, indicating that the enzyme can by-pass the branching points of beta-1,3-galactan backbones
-
-
?
methyl-beta-1,3-D-galactopentaoside + H2O
methyl-beta-1,3-D-galactotetraoside + D-galactose
-
relative activity: 100%. The enzyme hydolyzes beta-1,3-linked galactooligosaccharides, but not beta-1,6- and beta-1,4-linked galactooligosaccharides or alpha-1,3-linked galactobiose or beta-1,3-linked galactosylgalactosaminide
-
-
?
methyl-beta-1,3-D-galactopentaoside + H2O
methyl-beta-1,3-D-galactotetraoside + D-galactose
-
relative activity: 100%. The enzyme hydolyzes beta-1,3-linked galactooligosaccharides, but not beta-1,6- and beta-1,4-linked galactooligosaccharides or alpha-1,3-linked galactobiose or beta-1,3-linked galactosylgalactosaminide
-
-
?
methyl-beta-1,3-D-galactotetraoside + H2O
methyl-beta-1,3-D-galactotrioside + D-galactose
-
relative activity: 99%
-
-
?
methyl-beta-1,3-D-galactotetraoside + H2O
methyl-beta-1,3-D-galactotrioside + D-galactose
-
relative activity: 99%
-
-
?
additional information
?
-
the enzyme specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-D-galactotetraose. The enzyme also can perform beta-1-3 linked main chain hydrolysis in the presence of a beta-1,6 linked branch
-
-
?
additional information
?
-
-
the enzyme specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-D-galactotetraose. The enzyme also can perform beta-1-3 linked main chain hydrolysis in the presence of a beta-1,6 linked branch
-
-
?
additional information
?
-
the recombinant BbGal43A shows activity towards synthetic galactosides
-
-
?
additional information
?
-
the recombinant BbGal43A shows activity towards synthetic galactosides
-
-
?
additional information
?
-
the recombinant BbGal43A shows activity towards synthetic galactosides
-
-
?
additional information
?
-
-
the recombinant BbGal43A shows activity towards synthetic galactosides
-
-
?
additional information
?
-
the recombinant BLLJ_1840 expressed in Escherichia coli hydrolyzes beta-1,3-linked galactooligosaccharides but not beta-1,4- and beta-1,6-linked galactooligosaccharides. The enzyme also hydrolyzes larch wood arabinogalactan, which comprises a beta-1,3-linked galactan backbone with beta-1,6-linked galactan side chains. No activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-L-arabinopyranoside, substrate specificity, and no activity with potato galactan and laminarin, overview
-
-
?
additional information
?
-
the recombinant BLLJ_1840 expressed in Escherichia coli hydrolyzes beta-1,3-linked galactooligosaccharides but not beta-1,4- and beta-1,6-linked galactooligosaccharides. The enzyme also hydrolyzes larch wood arabinogalactan, which comprises a beta-1,3-linked galactan backbone with beta-1,6-linked galactan side chains. No activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-L-arabinopyranoside, substrate specificity, and no activity with potato galactan and laminarin, overview
-
-
?
additional information
?
-
the recombinant exo-beta-1,6-galactobiohydrolase specifically releases beta-1,6-galactobiose (beta-1,6-Gal2) from the nonreducing terminal of beta-1,6-galactooligosaccharides. beta-1,6-Gal2 is additively released from larch type II arabinogalactan (AG) by the combined use of type II AG degradative enzymes, including Bl1,3Gal, Bl1,6Gal, and BlArafA. GH30_5 exo-beta-1,6-galactobiohydrolase (Bl1,6Gal, EC 3.2.1.145) and GH43_22 alpha-L-arabinofuranosidase (BlArafA, EC 3.2.1.55) are degradative enzymes for type II arabinogalactan (AG) side chains in cooperation with GH43_24 exo-beta-1,3-galactanase (Bl1,3Gal, EC 3.2.1.145). Degradative mechanism, overview
-
-
?
additional information
?
-
no activity of the recombinant enzyme with 4-nitrophenyl beta-D-galactopyranoside, beta-1,4-D-galactobiose, or beta-1,6-D-galactobiose, and no activity with birchwood xylan, lupin galactan, carob galactomannan, sugar beet L-arabinan, and wheat arabinoxylan
-
-
?
additional information
?
-
-
no activity of the recombinant enzyme with 4-nitrophenyl beta-D-galactopyranoside, beta-1,4-D-galactobiose, or beta-1,6-D-galactobiose, and no activity with birchwood xylan, lupin galactan, carob galactomannan, sugar beet L-arabinan, and wheat arabinoxylan
-
-
?
additional information
?
-
no activity of the recombinant enzyme with 4-nitrophenyl beta-D-galactopyranoside, beta-1,4-D-galactobiose, or beta-1,6-D-galactobiose, and no activity with birchwood xylan, lupin galactan, carob galactomannan, sugar beet L-arabinan, and wheat arabinoxylan
-
-
?
additional information
?
-
-
no activity of the recombinant enzyme with 4-nitrophenyl beta-D-galactopyranoside, beta-1,4-D-galactobiose, or beta-1,6-D-galactobiose, and no activity with birchwood xylan, lupin galactan, carob galactomannan, sugar beet L-arabinan, and wheat arabinoxylan
-
-
?
additional information
?
-
-
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
-
-
?
additional information
?
-
-
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
-
-
?
additional information
?
-
specific hydrolysis of beta-1,3 and beta-1,6 galactooligosaccharides
-
-
?
additional information
?
-
-
specific hydrolysis of beta-1,3 and beta-1,6 galactooligosaccharides
-
-
?
additional information
?
-
-
no activity with lupin galactan, carob galactomannan, sugar beet L-arabinan, sugar beet debranched arabinan, wheat arabinoxylan, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl alpha-L-arabinopyranoside, and 4-nitrophenyl alpha-L-arabinofuranoside. The enzyme is not active on galactooligosaccharides with beta-1,4- or beta-1,6-linkages
-
-
?
additional information
?
-
-
no activity with lupin galactan, carob galactomannan, sugar beet L-arabinan, sugar beet debranched arabinan, wheat arabinoxylan, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl alpha-L-arabinopyranoside, and 4-nitrophenyl alpha-L-arabinofuranoside. The enzyme is not active on galactooligosaccharides with beta-1,4- or beta-1,6-linkages
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
-
-
?
additional information
?
-
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
-
-
?
additional information
?
-
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
-
-
?
additional information
?
-
-
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
-
-
?
additional information
?
-
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
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additional information
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the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
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physiological function
type II arabinogalactan (AG) degradative enzymes, including Bl1,3Gal, Bl1,6Gal, and BlArafA. GH30_5 exo-beta-1,6-galactobiohydrolase (Bl1,6Gal, EC 3.2.1.145) and GH43_22 alpha-L-arabinofuranosidase (BlArafA, EC 3.2.1.55) are important for the acquisition of type II AG in Bifidobacterium longum
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic relationships of BLLJ_1840
evolution
the enzyme belongs to the glycosyl hydrolase family 30, GH30, subfamily 22. GH43_24 exo-beta-1,3-galactanase (Bl1,3Gal, EC 3.2.1.145) forms a gene cluster with GH30_5 and GH43_22 enzyme candidates, which are conserved in all Bifidobacterium longum strains
evolution
the enzyme belongs to the glycosyl hydrolase family 43, GH43, subfamily 24. GH43_24 exo-beta-1,3-galactanase (Bl1,3Gal) forms a gene cluster with GH30_5 exo-beta-1,6-galactobiohydrolase (Bl1,6Gal) and GH43_22 alpha-L-arabinofuranosidase (BlArafA) enzyme candidates, which are conserved in all Bifidobacterium longum strains
evolution
the enzyme belongs to the glycosyl hydrolase family 43, GH43. Structure comparisons reveal that structural and sequence homology between BbGal43A, Clostridium thermocellum Ct1,3Gal43A (PDB ID 3vsf), and Bacteroides thetaiotaomicron BT2959 (PDB ID 3nqh) indicate that all three enzymes might be different types of exo-beta-1,3-galactanase
evolution
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the enzyme belongs to the glycosyl hydrolase family 43, GH43. Structure comparisons reveal that structural and sequence homology between BbGal43A, Clostridium thermocellum Ct1,3Gal43A (PDB ID 3vsf), and Bacteroides thetaiotaomicron BT2959 (PDB ID 3nqh) indicate that all three enzymes might be different types of exo-beta-1,3-galactanase
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evolution
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the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree
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evolution
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the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic relationships of BLLJ_1840
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evolution
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the enzyme belongs to the glycosyl hydrolase family 43, GH43. Structure comparisons reveal that structural and sequence homology between BbGal43A, Clostridium thermocellum Ct1,3Gal43A (PDB ID 3vsf), and Bacteroides thetaiotaomicron BT2959 (PDB ID 3nqh) indicate that all three enzymes might be different types of exo-beta-1,3-galactanase
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metabolism
the enzyme shows a synergistic effect with related enzymes on degradation of type II arabinogalactan
metabolism
GH30_5 exo-beta-1,6-galactobiohydrolase (Bl1,6Gal, EC 3.2.1.145) and GH43_22 alpha-L-arabinofuranosidase (BlArafA, EC 3.2.1.55) are degradative enzymes for type II arabinogalactan (AG) side chains in cooperation with GH43_24 exo-beta-1,3-galactanase (Bl1,3Gal, EC 3.2.1.145)
metabolism
GH30_5 exo-beta-1,6-galactobiohydrolase (Bl1,6Gal, EC 3.2.1.145) and GH43_22 alpha-L-arabinofuranosidase (BlArafA, EC 3.2.1.55), which are degradative enzymes for type II arabinogalactan (AG) side chains in cooperation with GH43_24 exo-beta-1,3-galactanase (Bl1,3Gal, EC 3.2.1.145)
metabolism
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the enzyme shows a synergistic effect with related enzymes on degradation of type II arabinogalactan
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additional information
domain structures of BLLJ_1840 comprising the GH43 catalytic domain, bacterial Ig-like domain, CBM32, and the LPXTG cell wall anchor domain (Anchor), as well as the signal peptide
additional information
two modes of substrate binding are observed at the beta site of the CtCBM13 domain, and one galactobiose molecule is found in an L shaped pocket of the CtGH43 domain, which appears large enough to accommodate two more galactose units. Glu112 serves as the general base for substrate hydrolysis. Putative mechanism of substrate delivery via the CBM13 domain, overview
additional information
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two modes of substrate binding are observed at the beta site of the CtCBM13 domain, and one galactobiose molecule is found in an L shaped pocket of the CtGH43 domain, which appears large enough to accommodate two more galactose units. Glu112 serves as the general base for substrate hydrolysis. Putative mechanism of substrate delivery via the CBM13 domain, overview
additional information
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domain structures of BLLJ_1840 comprising the GH43 catalytic domain, bacterial Ig-like domain, CBM32, and the LPXTG cell wall anchor domain (Anchor), as well as the signal peptide
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Tsumuraya, Y.; Mochizuki, N.; Hashimoto, Y.; Kovac, P.
Purification of an exo-beta-(1->3)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins
J. Biol. Chem.
265
7207-7215
1990
Irpex lacteus
brenda
Kotake, T.; Dina, S.; Konishi, T.; Kaneko, S.; Igarashi, K.; Samejima, M.; Watanabe, Y.; Kimura, K.; Tsumuraya, Y.
Molecular cloning of a b-galactosidase from radish that specifically hydrolyzes beta-(1->3)- and beta-(1->6)-galactosyl residues of arabinogalactan protein
Plant Physiol.
138
1563-1576
2005
Raphanus sativus (Q6L619), Raphanus sativus
brenda
Ichinose, H.; Kuno, A.; Kotake, T.; Yoshida, M.; Sakka, K.; Hirabayashi, J.; Tsumuraya, Y.; Kaneko, S.
Characterization of an exo-beta -1,3-galactanase from Clostridium thermocellum
Appl. Environ. Microbiol.
72
3515-3523
2006
Acetivibrio thermocellus (A3DD67), Acetivibrio thermocellus
brenda
Ichinose, H.; Kotake, T.; Tsumuraya, Y.; Kaneko, S.
Characterization of an exo-beta -1,3-D-galactanase from Streptomyces avermitilis NBRC14893 acting on arabinogalactan-proteins
Biosci. Biotechnol. Biochem.
70
2745-2750
2006
Streptomyces avermitilis, Streptomyces avermitilis NBRC 14893
brenda
Ling, N.; Pettolino, F.; Liao, M.; Bacic, A.
Preparation of a new chromogenic substrate to assay for beta-galactanases that hydrolyse type II arabino-3,6-galactans
Carbohydr. Res.
344
1941-1946
2009
Irpex lacteus
brenda
Ishida, T.; Fujimoto, Z.; Ichinose, H.; Igarashi, K.; Kaneko, S.; Samejima, M.
Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium
Acta Crystallogr. Sect. F
65
1274-1276
2009
Phanerodontia chrysosporium
brenda
Kotake, T.; Kitazawa, K.; Takata, R.; Okabe, K.; Ichingse, H.; Kaneko, S.; Tsumuraya, Y.
Molecular cloning and expression in Pichia pastoris of a Irpex lacteus exo-/beta-1,3-galactanase gene
Biosci. Biotechnol. Biochem.
73
2303-2309
2009
Irpex lacteus, Irpex lacteus NBRC 5367
brenda
Sakamoto, T.; Tanaka, H.; Nishimura, Y.; Ishimaru, M.; Kasai, N.
Characterization of an exo-beta-1,3-D-galactanase from Sphingomonas sp. 24T and its application to structural analysis of larch wood arabinogalactan
Appl. Microbiol. Biotechnol.
90
1701-1710
2011
Sphingomonas sp., Sphingomonas sp. 24T
brenda
Fujita, K.; Sakaguchi, T.; Sakamoto, A.; Shimokawa, M.; Kitahara, K.
Bifidobacterium longum subsp. longum exo-beta-1,3-galactanase, an enzyme for the degradation of type II arabinogalactan
Appl. Environ. Microbiol.
80
4577-4584
2014
Bifidobacterium longum (A0A061M1M5), Bifidobacterium longum JCM 1217 (A0A061M1M5)
brenda
Okawa, M.; Fukamachi, K.; Tanaka, H.; Sakamoto, T.
Identification of an exo-beta-1,3-D-galactanase from Fusarium oxysporum and the synergistic effect with related enzymes on degradation of type II arabinogalactan
Appl. Microbiol. Biotechnol.
97
9685-9694
2013
Fusarium oxysporum (B6F260), Fusarium oxysporum, Fusarium oxysporum 12S (B6F260), Fusarium oxysporum 12S
brenda
Ling, N.; Lee, J.; Ellis, M.; Liao, M.; Mau, S.; Guest, D.; Janssen, P.; Kovac, P.; Bacic, A.; Pettolino, F.
An exo-beta-(1->3)-D-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure
Carbohydr. Res.
352
70-81
2012
Streptomyces sp. (I0B0S9), Streptomyces sp. (I0B0T0), Streptomyces sp., Streptomyces sp. 19(2012) (I0B0S9), Streptomyces sp. 19(2012) (I0B0T0)
brenda
Jiang, D.; Fan, J.; Wang, X.; Zhao, Y.; Huang, B.; Liu, J.; Zhang, X.C.
Crystal structure of 1,3Gal43A, an exo-beta-1,3-galactanase from Clostridium thermocellum
J. Struct. Biol.
180
447-457
2012
Acetivibrio thermocellus (A3DD67), Acetivibrio thermocellus
brenda
Godoy, A.S.; de Lima, M.Z.; Camilo, C.M.; Polikarpov, I.
Crystal structure of a putative exo-beta-1,3-galactanase from Bifidobacterium bifidum S17
Acta Crystallogr. Sect. F
72
288-293
2016
Bifidobacterium bifidum (E4VCC5), Bifidobacterium bifidum S17 (E4VCC5), Bifidobacterium bifidum S17, Bifidobacterium bifidum NCIMB 41171 (E4VCC5)
brenda
Fujita, K.; Sakamoto, A.; Kaneko, S.; Kotake, T.; Tsumuraya, Y.; Kitahara, K.
Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum
Appl. Microbiol. Biotechnol.
103
1299-1310
2019
Bifidobacterium longum subsp. Longum (A0A401ETL2)
brenda