| Entry |
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| Name |
(Ara-f)3-Hyp beta-L-arabinobiosidase;
hypBA2 (gene name);
beta-L-arabinobiosidase
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| Class |
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
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| 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
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| 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]
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| Reaction(KEGG) |
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| 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]
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| Product |
4-O-(beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline [CPD: C20706];
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose [CPD: C20568]
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| 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.
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| History |
EC 3.2.1.187 created 2013
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| Orthology |
| K18206 | beta-L-arabinobiosidase |
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| Genes |
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| Reference |
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| Authors |
Fujita K, Sakamoto S, Ono Y, Wakao M, Suda Y, Kitahara K, Suganuma T |
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| Title |
Molecular cloning and characterization of a beta-L-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 3.2.1.187 |
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