| EC |
3.2.1.213 |
| Accepted name: |
galactan exo-1,6-β-galactobiohydrolase (non-reducing end) |
| Reaction: |
Hydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield (1→6)-β-galactobiose as the final product. |
| Other name(s): |
exo-β-1,6-galactobiohydrolase; 1,6Gal (gene name) |
| Systematic name: |
exo-β-(1→6)-galactobiohydrolase (non-reducing end) |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Fujita, K., Sakamoto, A., Kaneko, S., Kotake, T., Tsumuraya, Y. and Kitahara, K. Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum. Appl. Microbiol. Biotechnol. 103 (2019) 1299–1310. [PMID: 30564851] |
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| [EC 3.2.1.213 created 2020] |
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