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Literature summary for 3.4.23.5 extracted from
- Specificity of rat liver cathepsin D (1987), J. Biochem., 101, 575-580.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Hemoglobin + H2O | carboxymethyl-hemoglobin beta-chain | Rattus norvegicus | ? | - |
? |  |
| insulin + H2O | carboxylmethyl-insulin, cleavage sites | Rattus norvegicus | ? | - |
? | |
| lysozyme tryptide + H2O | cleavage sites | Rattus norvegicus | ? | - |
? | |
| additional information | at the P1 site the enzyme prefers hydrophobic residues except Ile and Val, that are branched at the beta-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively. A lower potency for beta-turn formation is essential for the sequence around the P1 site | Rattus norvegicus | ? | - |
? | |
| Myoglobin + H2O | cleavage sites | Rattus norvegicus | ? | - |
? | |
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Release 2023.1 (January 2023)
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