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 (1973) 393-8.
Reference
2
  Authors
Dey, P. M.
  Title
Further characterization of beta-L-arabinosidase from Cajanus indicus.
  Journal
Biochim.Biophys. Acta 746 (1983) 8-13.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39361-63-2

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