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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
Word Map
The expected taxonomic range for this enzyme is: Bifidobacterium longum
The taxonomic range for the selected organisms is: Bifidobacterium longum
Synonyms
beta-L-arabinofuranosidase, HypBA1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-L-arabinofuranosidase
299140
-
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, 37C
0.31
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
0.43
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
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, 37C
6.3
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
0.013
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
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, 37C
20
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
0.03
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
mutant E366A, pH 4.5, 37C
0.032
mutant E322A, pH 4.5, 37C
0.34
mutant E338A, pH 4.5, 37C
2.1
wild-type, pH 4.5, 37C
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, Bifidobacterium longum (E8MGH8)
Manually annotated by BRENDA team
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