We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.2.1.111 - 1,3-alpha-L-fucosidase for references in articles please use BRENDA:EC3.2.1.111Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hydrolysis of (1->3)-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-alpha-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase
Not identical with EC 3.2.1.63 1,2-alpha-L-fucosidase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
almond emulsin fucosidase I
-
-
-
-
alpha-L-fucosidase I
-
-
-
-
fucosidase, 1,3-alpha-L-
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
JCM1254
-
-
brenda
almond
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
lacto-N-difucohexaitol + H2O
?
-
poor substrate
-
-
?
lacto-N-fucopentaitol + H2O
?
lactoferrin + H2O
?
-
hydrolyzes only alpha-1,3-linkages between fucose and N-acetylglucosamine
-
-
?
additional information
?
-
lacto-N-fucopentaitol + 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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
no activation by Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
40% residual activity
Cu2+
-
complete inactiviation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NaCl
-
0.1 M, required for optimal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.101
lacto-N-fucopentaitol II
-
pH 5.0, 37°C
0.095
lacto-N-fucopentaitol III
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.46
L-Fuc-alpha-(1->3)-[D-Gal-beta-(1->4)]-D-Glc
-
pH 6.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4 - 6.8
-
about half-maximal activity at pH 4 and 6.8
4.3 - 5.8
-
about half-maximal activity at pH 4.3 and about 80% of maximal activity at pH 5.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
commercially available
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
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)
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
160000
-
2 * 160000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 160000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50
-
stable below, pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
decreasing ionic strength inactivates
-
freeze-thawing results in 30% loss of initial activity
-
major loss of activity by ion-exchange chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4°C, less than 10% loss of activity within 6 months
-
frozen, retains more than 90% of activity after 1 month
-
storage of lyophilized enzyme preparation results in 60% loss of activity within 1 month
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
affinity chromatography on Blue Sepharose; partial
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
I0DHK8_DROME
503
59160
TrEMBL
Q8A5P6_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
484
54625
TrEMBL
B7GNN8_BIFLS
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
478
53034
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
html completed