EC Number | Application | Comment | Organism |
---|---|---|---|
3.2.1.127 | analysis | the enzyme is potentially useful for glycan sequencing and analysis of more complex glycoconjugates | Bacteroides fragilis |
3.2.1.127 | medicine | using BfFucH coupled with endoglycosidases and the emerging glycosynthases allows glycoengineering of IgG antibodies to provide homogeneous glycoforms with well-defined glycan structures and optimal effector function | Bacteroides fragilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.127 | expressed in Escherichia coli from the CAZy database | Bacteroides fragilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.127 | Cu2+ | - |
Bacteroides fragilis | |
3.2.1.127 | Ni2+ | - |
Bacteroides fragilis | |
3.2.1.127 | Zn2+ | - |
Bacteroides fragilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.127 | 0.437 | - |
4-nitrophenyl alpha-L-fucopyranoside | pH 7.0, 37°C | Bacteroides fragilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.127 | Bacteroides fragilis | Q64R94 | - |
- |
3.2.1.127 | Bacteroides fragilis NCTC 9343 | Q64R94 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.127 | 4-nitrophenyl alpha-L-fucopyranoside + H2O | - |
Bacteroides fragilis | 4-nitrophenol + L-fucopyranose | - |
? | |
3.2.1.127 | 4-nitrophenyl alpha-L-fucopyranoside + H2O | - |
Bacteroides fragilis NCTC 9343 | 4-nitrophenol + L-fucopyranose | - |
? | |
3.2.1.127 | 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 | Bacteroides fragilis | ? | - |
? | |
3.2.1.127 | 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 | Bacteroides fragilis NCTC 9343 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.127 | BfFucH | - |
Bacteroides fragilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.127 | 60 | - |
- |
Bacteroides fragilis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.127 | 183.8 | - |
4-nitrophenyl alpha-L-fucopyranoside | pH 7.0, 37°C | Bacteroides fragilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.127 | 7 | 7.5 | - |
Bacteroides fragilis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.127 | 4.5 | 9 | pH 4.5: about 35% of maximal activity, pH 9.0: about 35% of maximal activity | Bacteroides fragilis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.127 | 420 | - |
4-nitrophenyl alpha-L-fucopyranoside | pH 7.0, 37°C | Bacteroides fragilis |