Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Clostridium perfringens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium perfringens | A0A0H2YQB3 | - |
- |
Clostridium perfringens | A0A0H2YQI3 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Clostridium perfringens |
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 | Comment | Organism |
---|---|---|
Afc2 | - |
Clostridium perfringens |
Afc3 | - |
Clostridium perfringens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Clostridium perfringens |
60 | - |
- |
Clostridium perfringens |
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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Clostridium perfringens |
8 | - |
- |
Clostridium perfringens |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 11 | stable | Clostridium perfringens |
5 | 11 | stable | Clostridium perfringens |
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 |