3.2.1.187: (Ara-f)3-Hyp beta-L-arabinobiosidase

This is an abbreviated version!
For detailed information about (Ara-f)3-Hyp beta-L-arabinobiosidase, go to the full flat file.

Reaction

Synonyms

beta-L-arabinobiosidase, beta-L-arabinofuranosidase, GH 121 beta-L-arabinofuranosidase, GH121 beta-L-arabinobiosidase, hypBA2, xcv2729, XeHypBA2

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.187 (Ara-f)3-Hyp beta-L-arabinobiosidase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
91	AA Sequence
2	Cloned(Commentary)
3	Expression
11	General Information
1	Inhibitors
1	KM Value [mM]
3	Localization
1	Metals/Ions
2	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
15	Organism
2	PDB ID
2	pH Optimum
3	Protein Variants
1	Purification (Commentary)
1	Reaction
7	Reference
19	Substrates and Products (Substrate)
7	Subunits
25	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Turnover Number [1/s]

Systematic Name

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Systematic Name on EC 3.2.1.187 - (Ara-f)3-Hyp beta-L-arabinobiosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Systematic Name Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SYSTEMATIC NAME

IUBMB Comments

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

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.