Entry Name (Ara-f)3-Hyp beta-L-arabinobiosidase;
Class Hydrolases;BRITE hierarchy
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) 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 Taxonomy Reference 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 Sequence Other DBs ExPASy - ENZYME nomenclature database: 3.2.1.187
