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Information on EC 3.2.1.111 - 1,3-alpha-L-fucosidase
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EC Tree
3.2.1.111 1,3-alpha-L-fucosidaseIUBMB Comments
Not identical with EC 3.2.1.63 1,2-alpha-L-fucosidase.
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Word Map
- 3.2.1.111
-
transfucosylation
- oligosaccharides
- lacto-n-tetraose
-
fucosylated
- perfringens
-
3.2.1.51
- lacto-n-fucopentaose
- milk
- glycoside
-
glycomics
- infant
- 3-fucosyllactose
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
bbafcb, cpafc2, cfase i, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AfcB
almond emulsin fucosidase I
-
-
-
-
alpha(1,3/4)-transfucosidase
alpha-1,3/4-L-fucosidase
alpha-L-fucosidase I
-
-
-
-
alphafuc
cFase I
core fucosidase I
fucosidase, 1,3-alpha-L-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Gal-beta-(1->4)-[Fuc-alpha-(1->3)]-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc-beta-R + H2O = Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc-beta-R + alpha-L-fucose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
83061-50-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-fucosyllactose + H2O
D-fucose + D-Gal-beta-(1->4)-D-Glc
-
-
-
?
asialoorosomucoid + H2O
?
-
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
-
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
-
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
-
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
-
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
-
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 +
-
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
-
i.e. Lewis a trisaccharide, 166% of the activity with 3-fucosyllactose
-
-
?
lactoferrin + H2O
?
-
hydrolyzes only alpha-1,3-linkages between fucose and N-acetylglucosamine
-
-
?
Lewis X trisaccharide + H2O
?
-
15448.5% activity compared to 4-nitrophenyl alpha-L-fucoside
-
-
?
3-fucosyllactose + H2O
L-fucose + lactose
-
1328.6% activity compared to 4-nitrophenyl alpha-L-fucoside
-
-
?
3-fucosyllactose + H2O
L-fucose + lactose
-
1328.6% activity compared to 4-nitrophenyl alpha-L-fucoside
-
-
?
3-O-fucosyllactose + 2'-fucosyllactose
lactodifucotetraose + ?
-
-
-
?
3-O-fucosyllactose + 2'-fucosyllactose
lactodifucotetraose + ?
-
-
-
?
3-O-fucosyllactose + lacto-N-fucopentaose I
lacto-N-difucohexaose + lactose
-
-
-
?
3-O-fucosyllactose + lacto-N-fucopentaose I
lacto-N-difucohexaose + lactose
-
-
-
?
3-O-fucosyllactose + lacto-N-neotetraose
lacto-N-fucopentaose III + lactose
-
-
-
?
3-O-fucosyllactose + lacto-N-neotetraose
lacto-N-fucopentaose III + lactose
-
-
-
?
3-O-fucosyllactose + lacto-N-tetraose
lacto-N-fucopentaose-II + lactose
-
-
-
?
3-O-fucosyllactose + lacto-N-tetraose
lacto-N-fucopentaose-II + lactose
-
-
-
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + L-fucose
-
100% activity
-
-
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + L-fucose
-
100% activity
-
-
?
4-nitrophenyl fucoside + H2O
4-nitrophenol + L-fucose
-
-
-
-
?
4-nitrophenyl fucoside + H2O
4-nitrophenol + L-fucose
-
-
-
-
?
horseradish type VI horseradish peroxidase + H2O
?
-
-
-
-
?
lacto-N-fucopentaitol + H2O
?
-
lacto-N-fucopentaitol II or III, no substrate: lacto-N-fucopentaitol I
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme specifically releases alpha-1,3- and alpha-1,4-linked fucosyl residues from 3-fucosyllactose, various Lewis blood group substances, and lacto-N-fucopentaose II and III. The enzyme does not act on glycoconjugates containing alpha-1,2-fucosyl residue or on synthetic alpha-fucoside, i.e. p-nitrophenyl-alpha-L-fucoside
-
-
?
additional information
?
-
the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate
-
-
?
additional information
?
-
-
the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate
-
-
?
additional information
?
-
the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate
-
-
?
additional information
?
-
-
the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl beta-L-fucoside, 4-nitrophenyl beta-D-fucoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl alpha-D-galactoside, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-lactoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl alpha-D-xyloside, 4-nitrophenyl beta-D-mannoside, 4-nitrophenyl alpha-D-mannoside, 4-nitrophenyl alpha-D-N-acetyl-glucoside, 4-nitrophenyl beta-D-N-acetyl-glucoside, 4-nitrophenyl alpha-D-N-acetyl-galactoside, 4-nitrophenyl beta-D-N-acetyl-galactoside, and 4-nitrophenyl alpha-D-N-acetyl-neuraminide. The enzyme is also inactive against 2'-fucsoyllactose, 6-fucosyl-N-acetylglucosamine, 6-fucosyl-N,N'-diacetylchitobiose, and Lewis A trisaccharide
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl beta-L-fucoside, 4-nitrophenyl beta-D-fucoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl alpha-D-galactoside, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-lactoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl alpha-D-xyloside, 4-nitrophenyl beta-D-mannoside, 4-nitrophenyl alpha-D-mannoside, 4-nitrophenyl alpha-D-N-acetyl-glucoside, 4-nitrophenyl beta-D-N-acetyl-glucoside, 4-nitrophenyl alpha-D-N-acetyl-galactoside, 4-nitrophenyl beta-D-N-acetyl-galactoside, and 4-nitrophenyl alpha-D-N-acetyl-neuraminide. The enzyme is also inactive against 2'-fucsoyllactose, 6-fucosyl-N-acetylglucosamine, 6-fucosyl-N,N'-diacetylchitobiose, and Lewis A trisaccharide
-
-
?
additional information
?
-
-
no hydrolysis of fucose alpha-1,6 or alpha-1,2-linkages to N-acetylglucosamine, as in IgG glycopeptides or 2'-fucosyllactitol
-
-
?
additional information
?
-
-
no substrates are alpha2-macroglobulin (MW 72600), bovine IgG glycopeptides or milk oligosaccharide 2'-fucosyllactose
-
-
?
additional information
?
-
-
the enzyme hydrolyzes fucose alpha-1,3 or alpha-1,4-linkages to N-acteylglucosamine
-
-
?
additional information
?
-
-
the enzyme hydrolyzes fucose alpha-1,3 or alpha-1,4-linkages to N-acteylglucosamine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme hydrolyzes fucose alpha-1,3 or alpha-1,4-linkages to N-acteylglucosamine
-
-
?
additional information
?
-
-
the enzyme hydrolyzes fucose alpha-1,3 or alpha-1,4-linkages to N-acteylglucosamine
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Mg2+, Mn2+, Ca2+, Ni2+, Fe2+, and Cd2+ have no significant effect on the enzymatic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by EDTA, urea or dithiothreitol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.1
3-fucosyllactose
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
5.1
3-fucosyllactose
-
mutant enzyme E315A, at pH 4.6 and 37°C
6.9
3-fucosyllactose
-
mutant enzyme C317S, at pH 4.6 and 37°C
0.5
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317A, at pH 4.6 and 37°C
0.5
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C467S, at pH 4.6 and 37°C
0.6
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317S, at pH 4.6 and 37°C
0.6
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C73S, at pH 4.6 and 37°C
0.6
4-nitrophenyl alpha-L-fucoside
-
wild type enzyme, at pH 4.6 and 37°C
1.2
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme E302A, at pH 4.6 and 37°C
1.3
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
17.4
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme D242A, at pH 4.6 and 37°C
1.3
Lewis X trisaccharide
-
wild type enzyme, at pH 4.6 and 37°C
1.5
Lewis X trisaccharide
-
mutant enzyme C467S, at pH 4.6 and 37°C
2.6
Lewis X trisaccharide
-
mutant enzyme C73S, at pH 4.6 and 37°C
2.8
Lewis X trisaccharide
-
mutant enzyme E315A, at pH 4.6 and 37°C
3.3
Lewis X trisaccharide
-
mutant enzyme C317A, at pH 4.6 and 37°C
4.1
Lewis X trisaccharide
-
mutant enzyme C317S, at pH 4.6 and 37°C
9.7
Lewis X trisaccharide
-
mutant enzyme D242A, at pH 4.6 and 37°C
12.8
Lewis X trisaccharide
-
mutant enzyme E302A, at pH 4.6 and 37°C
13.2
Lewis X trisaccharide
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
3-fucosyllactose
-
mutant enzyme E315A, at pH 4.6 and 37°C
1.34
3-fucosyllactose
-
mutant enzyme C317A, at pH 4.6 and 37°C
1.35
3-fucosyllactose
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
3.55
3-fucosyllactose
-
mutant enzyme C317S, at pH 4.6 and 37°C
3.87
3-fucosyllactose
-
mutant enzyme C73S, at pH 4.6 and 37°C
3.99
3-fucosyllactose
-
mutant enzyme C467S, at pH 4.6 and 37°C
0.00037
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme E302A, at pH 4.6 and 37°C
0.0004
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme D242A, at pH 4.6 and 37°C
0.013
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317A, at pH 4.6 and 37°C
0.022
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
0.062
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317S, at pH 4.6 and 37°C
0.127
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C467S, at pH 4.6 and 37°C
0.14
4-nitrophenyl alpha-L-fucoside
-
wild type enzyme, at pH 4.6 and 37°C
0.143
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C73S, at pH 4.6 and 37°C
0.078
Lewis X trisaccharide
-
mutant enzyme E315A, at pH 4.6 and 37°C
0.082
Lewis X trisaccharide
-
mutant enzyme D242A, at pH 4.6 and 37°C
0.23
Lewis X trisaccharide
-
mutant enzyme E302A, at pH 4.6 and 37°C
9.075
Lewis X trisaccharide
-
mutant enzyme C317A, at pH 4.6 and 37°C
21.55
Lewis X trisaccharide
-
wild type enzyme, at pH 4.6 and 37°C
23.83
Lewis X trisaccharide
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
25.43
Lewis X trisaccharide
-
mutant enzyme C467S, at pH 4.6 and 37°C
29.07
Lewis X trisaccharide
-
mutant enzyme C317S, at pH 4.6 and 37°C
34.47
Lewis X trisaccharide
-
mutant enzyme C73S, at pH 4.6 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
3-fucosyllactose
-
mutant enzyme E315A, at pH 4.6 and 37°C
0.328
3-fucosyllactose
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
0.45
3-fucosyllactose
-
mutant enzyme C317A, at pH 4.6 and 37°C
0.512
3-fucosyllactose
-
mutant enzyme C317S, at pH 4.6 and 37°C
0.723
3-fucosyllactose
-
mutant enzyme C73S, at pH 4.6 and 37°C
2.035
3-fucosyllactose
-
mutant enzyme C467S, at pH 4.6 and 37°C
0.000023
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme D242A, at pH 4.6 and 37°C
0.000317
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme E302A, at pH 4.6 and 37°C
0.017
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
0.027
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317A, at pH 4.6 and 37°C
0.1
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C317S, at pH 4.6 and 37°C
0.222
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C73S, at pH 4.6 and 37°C
0.232
4-nitrophenyl alpha-L-fucoside
-
wild type enzyme, at pH 4.6 and 37°C
0.248
4-nitrophenyl alpha-L-fucoside
-
mutant enzyme C467S, at pH 4.6 and 37°C
0.0083
Lewis X trisaccharide
-
mutant enzyme D242A, at pH 4.6 and 37°C
0.0183
Lewis X trisaccharide
-
mutant enzyme E302A, at pH 4.6 and 37°C
0.0283
Lewis X trisaccharide
-
mutant enzyme E315A, at pH 4.6 and 37°C
1.81
Lewis X trisaccharide
-
mutant enzyme 249DELTA265, at pH 4.6 and 37°C
2.77
Lewis X trisaccharide
-
mutant enzyme C317A, at pH 4.6 and 37°C
7.04
Lewis X trisaccharide
-
mutant enzyme C317S, at pH 4.6 and 37°C
13.06
Lewis X trisaccharide
-
mutant enzyme C73S, at pH 4.6 and 37°C
16.12
Lewis X trisaccharide
-
wild type enzyme, at pH 4.6 and 37°C
17.41
Lewis X trisaccharide
-
mutant enzyme C467S, at pH 4.6 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
-
about 85% activity at pH 4.0, about 60% activity at pH 5.0, about 45% activity at pH 6.0
4.3 - 5.8
-
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
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
</