| EC |
3.2.1.185 |
| Accepted name: |
non-reducing end β-L-arabinofuranosidase |
| Reaction: |
β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose + H2O = 2 β-L-arabinofuranose |
| Other name(s): |
HypBA1 |
| Systematic name: |
β-L-arabinofuranoside non-reducing end β-L-arabinofuranosidase |
| Comments: |
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K. and Suganuma, T. Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member. J. Biol. Chem. 289 (2014) 5240–5249. [DOI] [PMID: 24385433] |
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| [EC 3.2.1.185 created 2013] |
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