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Literature summary for 3.4.22.58 extracted from
- Identification of specific tethered inhibitors for caspase-5 (2012), Chem. Biol. Drug Des., 79, 209-215.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | identification of specific tethered inhibitors for caspase-5, screening, overview. A naphthyl-thiazole-containing molecule selectively inhibits and labels the allosteric cysteine in the p10 subunit of caspase-5, but causes very little inhibition or labeling of caspase-1. Some of allosteric tethered compounds to caspase-5 do not inhibit its enzymatic activity, suggesting that thiol-labeling itself is not sufficient to drive inhibition | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | allosteric site on caspase-5 | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
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Release 2023.1 (January 2023)
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