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Literature summary for 3.2.1.127 extracted from

  • 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 (2017), ACS Chem. Biol., 12, 63-72 .
    View publication on PubMed
Search for more literature for 3.2.1.127

Application

Application Comment Organism
analysis the enzyme is potentially useful for glycan sequencing and analysis of more complex glycoconjugates Bacteroides fragilis
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

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli from the CAZy database Bacteroides fragilis

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Bacteroides fragilis
Ni2+
-
 Bacteroides fragilis
Zn2+
-
 Bacteroides fragilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.437
-
 4-nitrophenyl alpha-L-fucopyranoside pH 7.0, 37°C Bacteroides fragilis

Organism

Organism UniProt Comment Textmining
Bacteroides fragilis Q64R94
-
-
Bacteroides fragilis NCTC 9343 Q64R94
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-L-fucopyranoside + H2O
-
 Bacteroides fragilis 4-nitrophenol + L-fucopyranose
-
 ?
4-nitrophenyl alpha-L-fucopyranoside + H2O
-
 Bacteroides fragilis NCTC 9343 4-nitrophenol + L-fucopyranose
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
BfFucH
-
 Bacteroides fragilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Bacteroides fragilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
183.8
-
 4-nitrophenyl alpha-L-fucopyranoside pH 7.0, 37°C Bacteroides fragilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5
-
 Bacteroides fragilis

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9 pH 4.5: about 35% of maximal activity, pH 9.0: about 35% of maximal activity Bacteroides fragilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
420
-
 4-nitrophenyl alpha-L-fucopyranoside pH 7.0, 37°C Bacteroides fragilis