KEGG   ENZYME: 3.2.1.187
Entry
EC 3.2.1.187                Enzyme                                 
Name
(Ara-f)3-Hyp beta-L-arabinobiosidase;
hypBA2 (gene name);
beta-L-arabinobiosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose hydrolase
Reaction(IUBMB)
4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-(beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose [RN:R10579]
Reaction(KEGG)
R10579
Substrate
4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline [CPD:C20705];
H2O [CPD:C00001]
Product
4-O-(beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline [CPD:C20706];
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose [CPD:C20568]
Comment
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, is specific for (Ara-f)3-Hyp, a sugar chain found in hydroxyproline-rich glyoproteins such as extensin and lectin. The enzyme was not able to accept (Ara-f)2-Hyp or (Ara-f)4-Hyp as substrates. In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
History
EC 3.2.1.187 created 2013
Orthology
K18206  beta-L-arabinobiosidase
Genes
ERM: EYR00_03260
BLO: BL0421
BLF: BLIF_0193
BLB: BBMN68_1163
BLM: BLLJ_0212
BLK: BLNIAS_02507
BLG: BIL_17390
BDE: BDP_1701(bbgIII)
BDN: BBDE_1611
Reference
1  [PMID:21149454]
  Authors
Fujita K, Sakamoto S, Ono Y, Wakao M, Suda Y, Kitahara K, Suganuma T
  Title
Molecular cloning and characterization of a beta-L-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family.
  Journal
J Biol Chem 286:5143-50 (2011)
DOI:10.1074/jbc.M110.190512
  Sequence
[blm:BLLJ_0212]
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.187
IUBMB Enzyme Nomenclature: 3.2.1.187
ExPASy - ENZYME nomenclature database: 3.2.1.187
BRENDA, the Enzyme Database: 3.2.1.187

  All links  
Protein sequence (648)   
   UniProt (80)   
   SWISS-PROT (1)   
   RefSeq(pep) (565)   
   PDBSTR (2)   
DNA sequence (1116)   
   RefSeq(nuc) (999)   
   GenBank (58)   
   EMBL (59)   
3D Structure (2)   
   PDB (2)   
Protein domain (8)   
   InterPro (8)   
All databases (1774)   

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