Information on EC 3.2.1.111 - 1,3-alpha-L-fucosidase

for references in articles please use BRENDA:EC3.2.1.111
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
3.2.1.111
-
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RECOMMENDED NAME
GeneOntology No.
1,3-alpha-L-fucosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->3)-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3-alpha-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase
Not identical with EC 3.2.1.63 1,2-alpha-L-fucosidase.
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CAS REGISTRY NUMBER
COMMENTARY hide
83061-50-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JCM1254
-
-
Manually annotated by BRENDA team
almond
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
Bifidobacteria are predominant bacteria present in the intestines of breast-fed infants and offer important health benefits for the host. alpha-L-Fucosidase AfcB play essential roles in degrading alpha1,3/4-fucosylated milk oligosaccharides, respectively, and also glycoconjugates, in the gastrointestinal tracts
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
asialoorosomucoid + H2O
?
show the reaction diagram
-
specifically hydrolyzes fucose in alpha-1,3-linkage to N-acetylglucosamine of Asn-linked oligosaccharide chain branches
-
-
?
L-Fuc-alpha-(1->2)-D-Gal-beta-(1->3)-[L-Fuc-alpha-(1->4)]-GlcNAc + H2O
L-fucose + L-Fuc-alpha-(1->2)-D-Gal-beta-(1->3)-D-GlcNAc
show the reaction diagram
-
i.e. Lewis b tetrasaccharide, 14% of the activity with 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->2)-D-Gal-beta-(1->4)-[L-Fuc-alpha-(1->3)]-D-GlcNAc + H2O
L-fucose + L-Fuc-alpha-(1->2)-D-Gal-beta-(1->4)-D-GlcNAc
show the reaction diagram
-
i.e. Lewis y tetrasaccharide, 128% of the activity with 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->3)-[D-Gal-beta-(1->4)]-D-Glc + H2O
L-fucose + D-Gal-beta-(1->4)-D-Glc
show the reaction diagram
-
i.e. 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->3)-[D-Gal-beta-(1->4)]-D-GlcNAc + H2O
L-fucose + D-Gal-beta-(1->4)-D-GlcNAc
show the reaction diagram
-
i.e. Lewis a trisaccharide, 160% of the activity with 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->3)-[D-Gal-beta-(1->4)]-D-GlcNAc-beta-(1->3)-D-Gal-beta-(1->4)-D-Glc + H2O
L-fucose + D-Gal-beta-(1->4)-D-GlcNAc-beta-(1->3)-D-Gal-beta-(1->4)-D-Glc
show the reaction diagram
-
i.e. lacto-N-fucopentaose III, 159% of the activity with 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->4)-D-Gal-beta-(1->3)-D-GlcNAc-beta-(1->3)-D-Gal-beta-(1->4)-D-Glc + H2O
L-fucose +
show the reaction diagram
-
i.e. lacto-N-fucopentaose II, 186% of the activity with 3-fucosyllactose
-
-
?
L-Fuc-alpha-(1->4)-[D-Gal-beta-(1->3)]-D-GlcNAc + H2O
L-fucose + D-Gal-beta-(1->3)-D-GlcNAc
show the reaction diagram
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i.e. Lewis a trisaccharide, 166% of the activity with 3-fucosyllactose
-
-
?
lacto-N-difucohexaitol + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
lacto-N-fucopentaitol + H2O
?
show the reaction diagram
lactoferrin + H2O
?
show the reaction diagram
-
hydrolyzes only alpha-1,3-linkages between fucose and N-acetylglucosamine
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
slight activation
Mg2+
-
slight activation
additional information
-
no activation by Mn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
40% residual activity
Cu2+
-
complete inactiviation
Hg2+
-
strong
L-fucose
-
-
malonate
-
above 20 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
0.1 M, required for optimal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.101
lacto-N-fucopentaitol II
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pH 5.0, 37°C
0.095
lacto-N-fucopentaitol III
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46
L-Fuc-alpha-(1->3)-[D-Gal-beta-(1->4)]-D-Glc
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pH 6.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00146
-
-
0.0645
-
-
additional information
-
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.8
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about half-maximal activity at pH 4 and 6.8
4.3 - 5.8
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about half-maximal activity at pH 4.3 and about 80% of maximal activity at pH 5.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482);
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
-
gel filtration
160000
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2 * 160000, SDS-PAGE
350000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 160000, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8
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stable
708607
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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stable below, pH 6.0
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
decreasing ionic strength inactivates
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freeze-thawing results in 30% loss of initial activity
-
major loss of activity by ion-exchange chromatography
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, less than 10% loss of activity within 6 months
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frozen, retains more than 90% of activity after 1 month
-
storage of lyophilized enzyme preparation results in 60% loss of activity within 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on Blue Sepharose; partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Introduction of afcB gene into the Bacterioides longum 105-A strain, which has no intrinsic alpha-L-fucosidase. The transformant is able to utilize 3-fucosyllactose and lacto-N-fucopentaose II as the sole carbon source
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
introduction of afcB gene into the Bacterioides longum 105-A strain, which has no intrinsic alpha-L-fucosidase. The transformant is able to utilize 3-fucosyllactose and lacto-N-fucopentaose II as the sole carbon source
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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.111)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)