3.2.1.145: galactan 1,3-beta-galactosidase
This is an abbreviated version!
For detailed information about galactan 1,3-beta-galactosidase, go to the full flat file.
Word Map on EC 3.2.1.145
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3.2.1.145
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glycoside
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galactose
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oligosaccharide
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carbohydrate-binding
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phanerochaete
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exo-acting
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chrysosporium
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larch
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beta-1,6-linked
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arabinofuranose
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thermocellum
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dockerin
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arabinogalactan-proteins
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pectic
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beta-1,3-linkage
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avermitilis
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galactooligosaccharides
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analysis
- 3.2.1.145
- glycoside
- galactose
- oligosaccharide
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carbohydrate-binding
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phanerochaete
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exo-acting
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chrysosporium
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larch
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beta-1,6-linked
- arabinofuranose
- thermocellum
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dockerin
- arabinogalactan-proteins
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pectic
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beta-1,3-linkage
- avermitilis
- galactooligosaccharides
- analysis
Reaction
Synonyms
arabinogalactan endo-1,3-beta-galactosidase, BbGal43A, beta-galactanase, Bl1,3Gal, Bl1,6Gal, BLLJ_1840, Ct1,3Gal43A, Cthe_0661, exo-/beta-1,3-galactanase, Exo-1,3-Gal, exo-beta-(1,3)-D-galactanase, exo-beta-(1->3)-D-galactanase, exo-beta-1,3-D -galactanase, exo-beta-1,3-D-galactanase, exo-beta-1,3-galactanase, exo-beta-1,6-galactobiohydrolase, Fo/1,3Gal, GH30_5 exo-beta-1,6-galactobiohydrolase, GH43_24 exo-beta-1,3-galactanase, Il1,3Gal, More, Pc1,3Gal43A, RsBGAL1, Sa1,3Gal43A, SGalase1, SGalase2
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Substrates Products
Substrates Products on EC 3.2.1.145 - galactan 1,3-beta-galactosidase
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REACTION DIAGRAM
alpha-L-arabinofuranosidase-treated root arabinogalactan proteins from radish + H2O
?
relative activity: 9.3
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?
beta-(1-6)-galactopentaose + H2O
beta-(1-6)-D-galactotetraose + D-galactose
50% of the activity with p-nitrophenyl-beta-galactoside
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-
?
beta-(1-6)-galactotetraose + H2O
beta-(1-6)-D-galactotriose + D-galactose
68% of the activity with p-nitrophenyl-beta-galactoside
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-
?
beta-(1-6)-galactotriose + H2O
beta-(1-6)-D-galactobiose + D-galactose
49% of the activity with p-nitrophenyl-beta-galactoside
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-
?
beta-1,3-beta-1,6-galactan + H2O
?
relative activity: 3.1%
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-
?
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
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-
?
beta-1,6-Gal3 + H2O
beta-1,6-Gal2 + D-galactose
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-
-
?
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
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-
?
beta-D-Gal-[(1->3)-beta-D-Gal]n + H2O
beta-D-Gal-[(1->3)-beta-D-Gal]n-1 + D-galactose
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only beta-(1, 3) oligomers act as substrates
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?
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
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-
?
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
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?
dearabinosylated larch wood arabinogalactan + H2O
?
best substrate
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?
dyed de-arabinosylated gum arabic + H2O
?
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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
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?
larch type II arabinogalactan + H2O
?
degradation profiles of type II AG
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?
larch type II arabinogalactan + H2O
beta-1,6-Gal2 + ?
release of galactobiose, beta-1,6-Gal2, degradation profiles of type II AG
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?
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 + ?
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the enzyme bypasses the branching points of beta-1,3-galactan backbones in larch wood arabinogalactan
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?
methyl-beta-1,3-D-galactopentaoside + H2O
methyl-beta-1,3-D-galactotetraoside + D-galactose
p-nitrophenyl-beta-galactoside + H2O
p-nitrophenol + beta-galactose
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-
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?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
8% of the activity with p-nitrophenyl-beta-galactoside
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?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
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the enzyme releases approximately 60% of the total D-galactose in the substrate
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?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
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the enzyme releases approximately 60% of the total D-galactose in the substrate
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?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
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relative activity: 100%. The enzyme hydrolizes only beta-1,3-linkage of two D-galactosyl residues at non-reducing ends of the substrate
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?
beta-(1-3)-D-galactan + H2O
beta-(1-3)-D-galactan + D-galactose
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relative activity: 100%. The enzyme hydrolizes only beta-1,3-linkage of two D-galactosyl residues at non-reducing ends of the substrate
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?
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
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?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
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?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
44% of the activity with p-nitrophenyl-beta-galactoside
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?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
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relative activity: 57%
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?
beta-(1-3)-D-galactotriose + H2O
beta-(1-3)-D-galactobiose + D-galactose
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relative activity: 57%
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?
D-galactose
relative activity: 31%
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?
beta-(1-3)-galactobiose + H2O
D-galactose
32% of the activity with p-nitrophenyl-beta-galactoside
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?
beta-(1-3)-galactobiose + H2O
D-galactose
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relative activity: 7.6%
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?
beta-(1-3)-galactobiose + H2O
D-galactose
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relative activity: 7.6%
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?
2 D-galactose
best beta-1,3-galactan substrate
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?
beta-1,3-D-galactobiose + H2O
2 D-galactose
best beta-1,3-galactan substrate
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?
beta-1,3-D-galactopentaose + H2O
D-galactose + ?
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?
beta-1,3-D-galactotetraose + H2O
D-galactose + ?
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?
beta-1,3-galactan + H2O
?
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best substrate, mode of action, overview
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?
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
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?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
preferred substrate
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?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose + D-galactose
preferred substrate
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?
D-galactose + beta-(1,3)-galactobiose
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?
beta-1,3-galactotriose + H2O
D-galactose + beta-(1,3)-galactobiose
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?
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
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?
dearabinosylated gum arabic + H2O
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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
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?
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
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?
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
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?
larch wood arabinogalactan + H2O
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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
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?
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
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?
methyl-beta-1,3-D-galactotetraoside + D-galactose
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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
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?
methyl-beta-1,3-D-galactopentaoside + H2O
methyl-beta-1,3-D-galactotetraoside + D-galactose
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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
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?
methyl-beta-1,3-D-galactotrioside + D-galactose
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relative activity: 99%
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?
methyl-beta-1,3-D-galactotetraoside + H2O
methyl-beta-1,3-D-galactotrioside + D-galactose
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relative activity: 99%
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?
?
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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
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?
additional information
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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
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?
additional information
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the recombinant BbGal43A shows activity towards synthetic galactosides
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additional information
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the recombinant BbGal43A shows activity towards synthetic galactosides
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additional information
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the recombinant BbGal43A shows activity towards synthetic galactosides
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additional information
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the recombinant BbGal43A shows activity towards synthetic galactosides
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additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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additional information
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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
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
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specific hydrolysis of beta-1,3 and beta-1,6 galactooligosaccharides
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?
additional information
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specific hydrolysis of beta-1,3 and beta-1,6 galactooligosaccharides
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?
additional information
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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
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?
additional information
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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
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?
additional information
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the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
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?
additional information
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the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
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?
additional information
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the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
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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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?
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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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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additional information
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the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
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additional information
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the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
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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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?
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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