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Literature summary for 3.5.3.15 extracted from
- Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1 (1999), J. Dermatol. Sci., 21, 113-126.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Rattus norvegicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| muscle | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| filaggrin + H2O | - |
Rattus norvegicus | ? + NH3 | - |
? | |
| keratin + H2O | peptidylarginine deiminase type I acts on the arginine residue in the V2 subdomain of mouse keratin more readily than peptidylarginine deiminase type II | Rattus norvegicus | ? + NH3 | - |
? | |
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Release 2023.1 (January 2023)
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