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ENZYME entry: EC 3.2.1.185

Accepted Name
Non-reducing end beta-L-arabinofuranosidase.
Reaction catalysed
Beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H(2)O <=> 2 beta-L-arabinofuranose
Comment(s)
  • The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the beta-L-arabinofuranose residue from the non-reducing end of multiple substrates, including beta-L- arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara(2)-Hyp, Ara(3)-Hyp, and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-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.
Cross-references
BRENDA3.2.1.185
EC2PDB3.2.1.185
ExplorEnz3.2.1.185
PRIAM enzyme-specific profiles3.2.1.185
KEGG Ligand Database for Enzyme Nomenclature3.2.1.185
IUBMB Enzyme Nomenclature3.2.1.185
IntEnz3.2.1.185
MEDLINEFind literature relating to 3.2.1.185
MetaCyc3.2.1.185
UniProtKB/Swiss-Prot
E8MGH8, HYBA1_BIFL2

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-