Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
2'-fucosyl-N-acetyllactosamine + H2O
alpha-L-fucose + ?
2-fucosyllactose + H2O
alpha-L-fucose + lactose
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
-
-
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucopyranose
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
alpha-1,6-fucosyl asialo-agalacto-fetuin + H2O
alpha-L-fucose + asialo-agalacto-fetuin
-
-
-
-
?
alpha-L-Fuc-(1->6)-beta-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
-
-
?
alpha-L-fucosyl asialo-agalacto-fetuin + H2O
alpha-L-fucose + asialo-agalacto-fetuin
-
-
-
-
?
immunglobulin G glycopeptide + H2O
?
-
good substrate
-
-
?
immunoglobulin G glycopeptide + H2O
fragments of immunoglobuline G glycopeptide
additional information
?
-
2'-fucosyl-N-acetyllactosamine + H2O
alpha-L-fucose + ?
-
-
-
?
2'-fucosyl-N-acetyllactosamine + H2O
alpha-L-fucose + ?
-
-
-
?
2-fucosyllactose + H2O
alpha-L-fucose + lactose
-
-
-
?
2-fucosyllactose + H2O
alpha-L-fucose + lactose
-
-
-
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucopyranose
-
-
-
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucopyranose
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
substrate incubated with plasma sample of breast cancer patients treated with anti-cancer monoclonal antibody trastuzumbal
-
-
?
immunoglobulin G glycopeptide + H2O
fragments of immunoglobuline G glycopeptide
-
-
-
-
?
immunoglobulin G glycopeptide + H2O
fragments of immunoglobuline G glycopeptide
-
-
alpha-1,6-fucosyl linkage is cleaved
?
additional information
?
-
-
alpha-1,2-, alpha-1,3- or alpha-1,4-alpha-L-fucosides are not cleaved, alpha-L-fucosyl asialo-fetuin is no substrate
-
-
?
additional information
?
-
the enzyme is capable of hydrolyzing fucosidic linkages, especially the alpha-1,6-linkage from the N-linked Fuc-alpha-1,6-GlcNAc residue on glycoproteins. A complete removal of terminal alpha-1,3 and alpha-1,4-linked fucose from the GlcNAc residue linked to the alpha-1,3 or the alpha-1,6 mannose arm of the N-glycans by BfFucH is observed. Short glycans with fucose alpha-1,3/4-linked to GlcNAc (LNFP III, and LN FP II) have very little cleavage activity (less than 5%), whereas the alpha-1,2 linkage to the galacose residue (LNFP I) is cleaved efficiently. Among the Lewis (Le) blood group antigens, Lea, Leb, Lex, and Ley, and sialyl Lex (sLex), only Ley, which has an alpha-1,2-linked fucose on the galactose and an alpha-1,3 linkage to the GlcNAc, show a complete cleavage of the alpha-1,2 linkage, while Leb, which has an alpha-1,2-linked fucose on the galactose in addition to the alpha-1,4-linked fucose on the GlcNAc, shows no cleavage activity at all, suggesting that the alpha-1,4-, but not the alpha-1,3-linked fucose cand block the enzyme from cleaving the alpha-1,2-linked fucose on galactose. Lea and Lex, the glycans with the fucose residue linked to the GlcNAc residue that are hindered by a terminal galactose, show no digestion either. No digestion of sLex. Complete digestion of the alpha-1,2-linked fucose on Globo H, a glycan used as an epitope for the synthesis of an anticancer vaccine. The enzyme can specifically hydrolyze the core fucose linkage of N-linked glycans, especially with an appreciable digestion rate toward the N-glycans with terminal sialylation. The enzyme can also cleave the alpha-1,2-linked fucose on galactose and alpha-1,3/4-linked fucose on GlcNAc when the GlcNAc is not capped with galactose
-
-
?
additional information
?
-
the enzyme is capable of hydrolyzing fucosidic linkages, especially the alpha-1,6-linkage from the N-linked Fuc-alpha-1,6-GlcNAc residue on glycoproteins. A complete removal of terminal alpha-1,3 and alpha-1,4-linked fucose from the GlcNAc residue linked to the alpha-1,3 or the alpha-1,6 mannose arm of the N-glycans by BfFucH is observed. Short glycans with fucose alpha-1,3/4-linked to GlcNAc (LNFP III, and LN FP II) have very little cleavage activity (less than 5%), whereas the alpha-1,2 linkage to the galacose residue (LNFP I) is cleaved efficiently. Among the Lewis (Le) blood group antigens, Lea, Leb, Lex, and Ley, and sialyl Lex (sLex), only Ley, which has an alpha-1,2-linked fucose on the galactose and an alpha-1,3 linkage to the GlcNAc, show a complete cleavage of the alpha-1,2 linkage, while Leb, which has an alpha-1,2-linked fucose on the galactose in addition to the alpha-1,4-linked fucose on the GlcNAc, shows no cleavage activity at all, suggesting that the alpha-1,4-, but not the alpha-1,3-linked fucose cand block the enzyme from cleaving the alpha-1,2-linked fucose on galactose. Lea and Lex, the glycans with the fucose residue linked to the GlcNAc residue that are hindered by a terminal galactose, show no digestion either. No digestion of sLex. Complete digestion of the alpha-1,2-linked fucose on Globo H, a glycan used as an epitope for the synthesis of an anticancer vaccine. The enzyme can specifically hydrolyze the core fucose linkage of N-linked glycans, especially with an appreciable digestion rate toward the N-glycans with terminal sialylation. The enzyme can also cleave the alpha-1,2-linked fucose on galactose and alpha-1,3/4-linked fucose on GlcNAc when the GlcNAc is not capped with galactose
-
-
?
additional information
?
-
the enzyme is a alpha(1,2)-fucosidase that also possesses alpha(1,6) specificity on small unbranched substrates. It is active on mucin after sialidase-catalyzed removal of terminal sialic acid residues and also removes fucose from blood group H. The alpha(1,3) and alpha(1,4) linkages are not cleaved on 3-fucosyllactose and the Lewis A trisaccharide, respectively. The enzyme is also inactive on the substrate alpha-L-Fuc-(1,4)-beta-D-Gal
-
-
?
additional information
?
-
the enzyme is a alpha(1,2)-fucosidase that also possesses alpha(1,6) specificity on small unbranched substrates. It is active on mucin after sialidase-catalyzed removal of terminal sialic acid residues and also removes fucose from blood group H. The alpha(1,3) and alpha(1,4) linkages are not cleaved on 3-fucosyllactose and the Lewis A trisaccharide, respectively. The enzyme is also inactive on the substrate alpha-L-Fuc-(1,4)-beta-D-Gal
-
-
?
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.
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.
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.
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.
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.
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.
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.
Yazawa, S.; Madiyalakan, R.; Chawda, R.P.; Matta, K.L.
alpha-L-Fucosidase from Aspergillus niger: demonstration of a novel alpha-L-(1--6)-fucosidase acting on glycopeptides
Biochem. Biophys. Res. Commun.
136
563-569
1986
Aspergillus niger
brenda
Rosano, C.; Zuccotti, S.; Cobucci-Ponzano, B.; Mazzone, M.; Rossi, M.; Moracci, M.; Petoukhov, M.V.; Svergun, D.I.; Bolognesi, M.
Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchroton small angle X-ray scattering
Biochem. Biophys. Res. Commun.
320
176-182
2004
Saccharolobus solfataricus
brenda
Matsumoto, K.; Shimizu, C.; Arao, T.; Andoh, M.; Katsumata, N.; Kohno, T.; Yonemori, K.; Koizumi, F.; Yokote, H.; Aogi, K.; Tamura, K.; Nishio, K.; Fujiwara, Y.
Identification of predictive biomarkers for response to trastuzumab using plasma FUCA activity and N-glycan identified by MALDI-TOF-MS
J. Proteome Res.
8
457-462
2009
Homo sapiens
brenda
Grass, J.; Pabst, M.; Kolarich, D.; Poeltl, G.; Leonard, R.; Brecker, L.; Altmann, F.
Discovery and structural characterization of fucosylated oligomannosidic N-glycans in mushrooms
J. Biol. Chem.
286
5977-5984
2011
Bos taurus
brenda
Tsai, T.I.; Li, S.T.; Liu, C.P.; Chen, K.Y.; Shivatare, S.S.; Lin, C.W.; Liao, S.F.; Lin, C.W.; Hsu, T.L.; Wu, Y.T.; Tsai, M.H.; Lai, M.Y.; Lin, N.H.; Wu, C.Y.; Wong, C.H.
An effective bacterial fucosidase for glycoprotein remodeling
ACS Chem. Biol.
12
63-72
2017
Bacteroides fragilis (Q64R94), Bacteroides fragilis NCTC 9343 (Q64R94)
brenda
Megson, Z.A.; Koerdt, A.; Schuster, H.; Ludwig, R.; Janesch, B.; Frey, A.; Naylor, K.; Wilson, I.B.; Stafford, G.P.; Messner, P.; Schaeffer, C.
Characterization of an alpha-L-fucosidase from the periodontal pathogen Tannerella forsythia
Virulence
6
282-292
2015
Tannerella forsythia (G8UMQ6), Tannerella forsythia ATCC 43037 (G8UMQ6)
brenda