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Information on EC 3.2.1.111 - 1,3-alpha-L-fucosidase
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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
- oligosaccharides
-
transfucosylation
- lacto-n-fucopentaose
- lacto-n-tetraose
-
fucosylated
- infant
- 3-fucosyllactose
-
3.2.1.51
- glycoside
- perfringens
- milk
-
glycomics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
AfcB, almond emulsin fucosidase I, alpha(1,3/4)-transfucosidase, alpha-1,3/4-L-fucosidase, alpha-L-fucosidase I, alphafuc, BbAfcB, cFase I, core fucosidase I, CpAfc2, 
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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
Hydrolysis of (1->3)-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins
-
-
-
-
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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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). I0DHK8_DROME
503
1
59160
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H2YQI3_CLOP1
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
932
0
103826
TrEMBL
-
B7GNN8_BIFLS
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
478
0
53034
TrEMBL
-
Q8A5P6_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
484
0
54625
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F34H/L321P
the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
F34I/L321P
the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
F34Y/L321P
the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
L321P
the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
F34H/L321P
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the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
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F34I/L321P
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the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
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F34Y/L321P
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the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
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L321P
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the mutant exhibits increased transfucosylation activity compared to the wild type enzyme
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249DELTA265
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the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (14fold) 3-fucosyllactose (5fold) and Lewis X trisaccharide (9fold) compared to the wild type enzyme
C317A
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the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (9fold) 3-fucosyllactose (4fold) and Lewis X trisaccharide (6fold) compared to the wild type enzyme
C317S
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the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (2fold) 3-fucosyllactose (3fold) and Lewis X trisaccharide (2fold) compared to the wild type enzyme
C467S
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the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (0.9fold) 3-fucosyllactose (0.9fold) and Lewis X trisaccharide (9fold) compared to the wild type enzyme
C73S
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the mutant shows wild type activity with 4-nitrophenyl alpha-L-fucoside and Lewis X trisaccharide and shows decreased activity with 3-fucosyllactose (2fold) compared to the wild type enzyme
D242A
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the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (10000fold) and Lewis X trisaccharide (1928fold) compared to the wild type enzyme
E302A
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the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (736fold) and Lewis X trisaccharide (900fold) compared to the wild type enzyme
E315A
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the mutant is inactive with 4-nitrophenyl alpha-L-fucoside and shows decreased activity with 3-fucosyllactose (473fold) and Lewis X trisaccharide (585fold) compared to the wild type enzyme
C317S
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the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (2fold) 3-fucosyllactose (3fold) and Lewis X trisaccharide (2fold) compared to the wild type enzyme
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C73S
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the mutant shows wild type activity with 4-nitrophenyl alpha-L-fucoside and Lewis X trisaccharide and shows decreased activity with 3-fucosyllactose (2fold) compared to the wild type enzyme
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D242A
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the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (10000fold) and Lewis X trisaccharide (1928fold) compared to the wild type enzyme
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E302A
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the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (736fold) and Lewis X trisaccharide (900fold) compared to the wild type enzyme
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E315A
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the mutant is inactive with 4-nitrophenyl alpha-L-fucoside and shows decreased activity with 3-fucosyllactose (473fold) and Lewis X trisaccharide (585fold) compared to the wild type enzyme
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additional information
additional information
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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
additional information
replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%)
additional information
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replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%)
additional information
replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%)
additional information
-
replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
storage of lyophilized enzyme preparation results in 60% loss of activity within 1 month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3)
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshima, H.; Takasaki, S.; Ito-Mega, S.; Kobata, A.
Purification of almond emulsin alpha-L-fucosidase I by affinity chromatography
Arch. Biochem. Biophys.
194
394-398
1979
Prunus dulcis
brenda
Ogata-Arakawa, M.; Muramatsu, T.; Kobata, A.
alpha-L-Fucosidases from almond emulsin: characterization of the two enzymes with different specificities
Arch. Biochem. Biophys.
181
353-358
1977
Prunus dulcis
brenda
Imbert, M.J.; Glasgow, L.R.; Pizzo, S.V.
Purification of an almond emulsin fucosidase on Cibacron blue-Sepharose and demonstration of its activity toward fucose-containing glycoproteins
J. Biol. Chem.
257
8205-8210
1982
Prunus dulcis
brenda
Ashida, H.; Miyake, A.; Kiyohara, M.; Wada, J.; Yoshida, E.; Kumagai, H.; Katayama, T.; Yamamoto, K.
Two distinct alpha-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates
Glycobiology
19
1010-1017
2009
Bifidobacterium bifidum
brenda
Zeuner, B.; Vuillemin, M.; Holck, J.; Muschiol, J.; Meyer, A.S.
Loop engineering of an alpha-1,3/4-L-fucosidase for improved synthesis of human milk oligosaccharides
Enzyme Microb. Technol.
115
37-44
2018
Clostridium perfringens (A0A0H2YQI3), Clostridium perfringens, Bifidobacterium bifidum (C5NS94), Bifidobacterium bifidum
brenda
Saumonneau, A.; Champion, E.; Peltier-Pain, P.; Molnar-Gabor, D.; Hendrickx, J.; Tran, V.; Hederos, M.; Dekany, G.; Tellier, C.
Design of an alpha-L-transfucosidase for the synthesis of fucosylated HMOs
Glycobiology
26
261-269
2016
Bifidobacterium longum subsp. infantis (B7GNN8), Bifidobacterium longum subsp. infantis ATCC 15697 (B7GNN8)
brenda
Li, T.; Li, M.; Hou, L.; Guo, Y.; Wang, L.; Sun, G.; Chen, L.
Identification and characterization of a core fucosidase from the bacterium Elizabethkingia meningoseptica
J. Biol. Chem.
293
1243-1258
2018
Elizabethkingia meningoseptica, Elizabethkingia meningoseptica FMS-007
brenda
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