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Literature summary for 3.4.22.14 extracted from
- Actinidain-hydrolyzed type I collagen reveals a crucial amino acid sequence in fibril formation (2010), J. Biol. Chem., 285, 17465-17470.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Actinidia deliciosa | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Actinidia deliciosa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen type I + H2O | actinidain cleaves between Gly1032 and Gly1033, limited hydrolysis by actinidain protease produces monomeric collagen, which consisted almost entirely of alpha1 and alpha2 chains | Actinidia deliciosa | ? | - |
? |  |
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Release 2023.1 (January 2023)
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