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Literature summary for 3.2.1.51 extracted from

  • Fan, S.; Zhang, H.; Chen, X.; Lu, L.; Xu, L.; Xiao, M.
    Cloning, characterization, and production of three alpha-L-fucosidases from Clostridium perfringens ATCC 13124 (2016), J. Basic Microbiol., 56, 347-357 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Clostridium perfringens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.46
-
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc pH 7, 37°C Clostridium perfringens
3.1
-
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc pH 7, 37°C Clostridium perfringens
6.01
-
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose pH 7, 37°C Clostridium perfringens

Organism

Organism UniProt Comment Textmining
Clostridium perfringens A0A0H2YQB3
-
-
Clostridium perfringens A0A0H2YQI3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Clostridium perfringens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose + H2O the enzyme does not hydrolyze other fucosyloligosaccharides or 4-nitrophenyl-alpha-L-fucoside Clostridium perfringens alpha-L-fucose + D-galactose
-
?
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc + H2O i.e. Le(x) trisaccharide Clostridium perfringens alpha-L-fucose + beta-D-Gal-(1->3)-D-GlcNAc
-
?
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc + H2O i.e. Le(a) trisaccharide Clostridium perfringens alpha-L-fucose + beta-D-Gal-(1->4)-D-GlcNAc
-
?
additional information Afc2 shows enzyme activities exclusively to Le(x) trisaccharide and Le(a) trisaccharide. Although 3-fucosyl-GlcNAc and 4-fucosyl-GlcNAc have the same fucosyl linkage with Le(x) or Le(a) trisaccharides, they are resistant to the hydrolysis by Afc2 because they do not have the branched Gal residues at the non-reducing end. Afc2 is a 1,3-1,4-alphs-L-fucosidase Clostridium perfringens ?
-
?

Synonyms

Synonyms Comment Organism
Afc2
-
Clostridium perfringens
Afc3
-
Clostridium perfringens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Clostridium perfringens
60
-
-
Clostridium perfringens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
30 min, the enzyme maintains over 75% enzyme activity below 55°C Clostridium perfringens
55
-
the enzyme maintains over 95% enzyme activity below 55°C Clostridium perfringens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
15.4
-
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose pH 7, 37°C Clostridium perfringens
23.6
-
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc pH 7, 37°C Clostridium perfringens
26.9
-
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc pH 7, 37°C Clostridium perfringens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Clostridium perfringens
8
-
-
Clostridium perfringens

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 11 stable Clostridium perfringens
5 11 stable Clostridium perfringens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.56
-
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose pH 7, 37°C Clostridium perfringens
8.66
-
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc pH 7, 37°C Clostridium perfringens
9.56
-
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc pH 7, 37°C Clostridium perfringens