KEGG   ENZYME: 3.2.1.185Help
Entry
EC 3.2.1.185                Enzyme                                 

Name
non-reducing end beta-L-arabinofuranosidase;
HypBA1
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
beta-L-arabinofuranoside non-reducing end beta-L-arabinofuranosidase
Reaction(IUBMB)
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose [RN:R10346]
Reaction(KEGG)
Substrate
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose [CPD:C20568];
H2O [CPD:C00001]
Product
beta-L-arabinofuranose [CPD:C20569]
Comment
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), Ara2-Hyp, Ara3-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, non-reducing end alpha-L-arabinofuranosidase
History
EC 3.2.1.185 created 2013
Orthology
K18205  
non-reducing end beta-L-arabinofuranosidase
Genes
BLO: 
BLF: 
BLB: 
BLM: 
BLK: 
BLG: 
BLZ: 
BADO: 
BLA: 
BLC: 
BLT: 
BBB: 
BBC: 
BNM: 
BLV: 
BLW: 
BLS: 
BANI: 
BANL: 
BANM: 
BDE: 
BDN: 
BBRE: 
BBRV: 
BBRN: 
BBRS: 
BCAT: 
BPSC: 
BSCA: 
 » show all
Taxonomy
Reference
1  [PMID:21914802]
  Authors
Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T
  Title
Characterization of a novel beta-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member.
  Journal
J. Biol. Chem. 286 (2011) 38079-85.
  Sequence
[blm:BLLJ_0211]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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