3.2.1.127: 1,6-alpha-L-fucosidase
This is an abbreviated version!
For detailed information about 1,6-alpha-L-fucosidase, go to the full flat file.
Reaction
Synonyms
alpha-L fucosidase, alpha-L-fucosidase, BfFucH, bfo_2737, FucA, fucosidase, 1,6-alpha-L-, Ss-alpha-fuc, TfFuc1
ECTree
3.2.1.127 1,6-alpha-L-fucosidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.127 - 1,6-alpha-L-fucosidase
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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
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
-
-
?
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
-
-
-
-
?
2'-fucosyl-N-acetyllactosamine + H2O
alpha-L-fucose + ?
-
-
-
?
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
-
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
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-
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
-
-
?
