The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1→6)-β-galactobiose from the non-reducing terminal of (1→6)-β-D-galactooligosaccharides with a degree of polymerization (DP) of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse α-L-arabinofuranosylated (1→6)-β-galactans (as found in arabinogalactans) and does not act on (1→3)-β-D- or (1→4)-β-D-galactans. cf. EC 3.2.1.164, galactan endo-1,6-β-galactosidase.
The expected taxonomic range for this enzyme is: Bifidobacterium longum subsp. longum
Hydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield (1->6)-beta-galactobiose as the final product.
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield (1->6)-beta-galactobiose as the final product.
The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1->6)-beta-galactobiose from the non-reducing terminal of (1->6)-beta-D-galactooligosaccharides with a degree of polymerization (DP) of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse alpha-L-arabinofuranosylated (1->6)-beta-galactans (as found in arabinogalactans) and does not act on (1->3)-beta-D- or (1->4)-beta-D-galactans. cf. EC 3.2.1.164, galactan endo-1,6-beta-galactosidase.
Substrates: degradative enzyme for type II arabinogalactan side chains in cooperation with exo-beta-1,3-galactanase. The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1->6)-beta-galactobiose from the non-reducing terminal of (1->6)-beta-D-galactooligosaccharides with a degree of polymerization of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse alpha-L-arabinofuranosylated (1->6)-beta-galactans (as found in arabinogalactans) and does not act on (1->3)-beta-D- or (1->4)-beta-D-galactans Products: -
Substrates: the enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1->6)-beta-galactobiose from the non-reducing terminal of (1->6)-beta-D-galactooligosaccharides with a degree of polymerization of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse alpha-L-arabinofuranosylated (1->6)-beta-galactans (as found in arabinogalactans) and does not act on (1->3)-beta-D- or (1->4)-beta-D-galactans Products: -
Substrates: degradative enzyme for type II arabinogalactan side chains in cooperation with exo-beta-1,3-galactanase. The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1->6)-beta-galactobiose from the non-reducing terminal of (1->6)-beta-D-galactooligosaccharides with a degree of polymerization of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse alpha-L-arabinofuranosylated (1->6)-beta-galactans (as found in arabinogalactans) and does not act on (1->3)-beta-D- or (1->4)-beta-D-galactans Products: -