Application | Comment | Organism |
---|---|---|
medicine | potential application in the field of erythrocyte conversion technology | Clostridium perfringens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.35 | - |
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide | pH 7.0, 37°C | Clostridium perfringens | |
1.58 | - |
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide | pH 7.0, 37°C | Clostridium perfringens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
72100 | - |
x * 72100 Da, SDS-PAGE | Clostridium perfringens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium perfringens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Clostridium perfringens |
Source Tissue | Comment | Organism | Textmining |
---|
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
43.92 | - |
- |
Clostridium perfringens |
Storage Stability | Organism |
---|---|
4°C, 12 months | Clostridium perfringens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is highly selective for terminal N-acetylgalactosamine residues, sugars other than N-acetyl-alpha-D-galactosaminide are not substrates. the enzyme degrades blood A epitope | Clostridium perfringens | ? | - |
? | |
o-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O | - |
Clostridium perfringens | o-nitrophenol + N-acetyl-alpha-D-galactosamine | - |
? | |
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O | - |
Clostridium perfringens | p-nitrophenol + N-acetyl-alpha-D-galactosamine | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 72100 Da, SDS-PAGE | Clostridium perfringens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7 | - |
Clostridium perfringens |