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Information on EC 3.2.1.185 - non-reducing end beta-L-arabinofuranosidase and Organism(s) Bifidobacterium longum and UniProt Accession E8MGH8

for references in articles please use BRENDA:EC3.2.1.185
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EC Tree
IUBMB Comments
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
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This record set is specific for:
Bifidobacterium longum
UNIPROT: E8MGH8
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The taxonomic range for the selected organisms is: Bifidobacterium longum
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hypba1, xcv2724, xehypba1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-L-arabinofuranosidase
-
HypBA1
-
-
-
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
show the reaction diagram
-
enzyme liberates L-arabinose from the L-arabinofuranose (Ara)-beta1,2-Ara disaccharide
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline + H2O
2 beta-L-arabinofuranose + L-hydroxyproline
show the reaction diagram
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
0.31
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.43
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
6.3
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.013
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
20
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.03
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
mutant E366A, pH 4.5, 37°C
0.032
mutant E322A, pH 4.5, 37°C
0.34
mutant E338A, pH 4.5, 37°C
2.1
wild-type, pH 4.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
x * 74000, SDS-PAGE, x * 74319, calculated
74319
x * 74000, SDS-PAGE, x * 74319, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 74000, SDS-PAGE, x * 74319, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E322A
1.5% of wild-type activity
E338A
16% of wild-type activity
E366A
0.0013% of wild-type activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, K.; Takashi, Y.; Obuchi, E.; Kitahara, K.; Suganuma, T.
Characterization of a novel ?-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member
J. Biol. Chem.
286
38079-38085
2011
Bifidobacterium longum (E8MGH8), Bifidobacterium longum
Manually annotated by BRENDA team