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Literature summary for 3.2.1.49 extracted from
- Clostridium perfringens alpha-N-acetylgalactosaminidase blood group A2-degrading activity (2003), Biotechnol. Appl. Biochem., 37, 157-163.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | the enzyme may be useful for enzymic conversion of type A2 to universally transfusable type O red blood cells, potential application in the field of solid organ transplantation | Clostridium perfringens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium perfringens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme hydrolyzes the terminal N-actyl-alpha-D-galactosamine from the blood type A2 antigen producing H antigen, blood type O | Clostridium perfringens | ? | - |
? |  |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 4 | 37 | the enzyme hydrolyses A2 epitopes at 4°C with 42% of the efficiency of that at 37°C | Clostridium perfringens |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | 27% decline in activity from pH 6.0-8.0 with no apparent optimum | Clostridium perfringens |
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