KEGG   ENZYME: 3.2.1.88Help
Entry
EC 3.2.1.88                 Enzyme                                 

Name
non-reducing end beta-L-arabinopyranosidase;
vicianosidase;
beta-L-arabinosidase (ambiguous);
beta-L-arabinoside arabinohydrolase (ambiguous)
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
beta-L-arabinopyranoside non-reducing end beta-L-arabinopyranosidase
Reaction(IUBMB)
Removal of a terminal beta-L-arabinopyranose residue from the non-reducing end of its substrate. [RN:R01760]
Reaction(KEGG)
Comment
The enzyme, which was characterized from dormant seeds of the plant Cajanus cajan (pigeon pea), has been shown to remove the terminal non-reducing beta-L-arabinopyranoside residue from the artificial substrate p-nitrophenyl-beta-L-arabinopyranose [1]. In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-beta-L-arabinopyranose [2].
History
EC 3.2.1.88 created 1976, modified 2013
Reference
1  [PMID:4699248]
  Authors
Dey PM.
  Title
Beta-L-arabinosidase from Cajanus indicus: a new enzyme.
  Journal
Biochim Biophys Acta 302:393-8 (1973)
DOI:10.1016/0005-2744(73)90167-8
Reference
2
  Authors
Dey, P. M.
  Title
Further characterization of beta-L-arabinosidase from Cajanus indicus.
  Journal
BiochimBiophys Acta 746:8-13 (1983)
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.88
IUBMB Enzyme Nomenclature: 3.2.1.88
ExPASy - ENZYME nomenclature database: 3.2.1.88
BRENDA, the Enzyme Database: 3.2.1.88
CAS: 39361-63-2

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