3.2.1.185: non-reducing end beta-L-arabinofuranosidase

This is an abbreviated version!
For detailed information about non-reducing end beta-L-arabinofuranosidase, go to the full flat file.

Reaction

Synonyms

beta-L-arabinofuranosidase, GH 127 beta-L-arabinofuranosidase, GH127 beta-L-arabinofuranosidase, HypBA1, xcv2724, XeHypBA1

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.185 non-reducing end beta-L-arabinofuranosidase

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Results	in table
416	AA Sequence
1	Cloned(Commentary)
3	Expression
9	General Information
3	kcat/KM [mM/s]
3	KM Value [mM]
3	Localization
2	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
4	Organism
11	PDB ID
2	pH Optimum
6	Protein Variants
1	Reaction
4	Reference
4	Specific Activity [micromol/min/mg]
14	Substrates and Products (Substrate)
1	Subunits
18	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
3	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 3.2.1.185 - non-reducing end beta-L-arabinofuranosidase

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SYSTEMATIC NAME

IUBMB Comments

beta-L-arabinofuranoside non-reducing end beta-L-arabinofuranosidase

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