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Literature summary for 3.4.25.1 extracted from
- Conformational and enzymatic changes of 20S proteasome of rat natural killer cells induced by mono- and divalent cations (2004), J. Struct. Biol., 145, 263-271.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| SDS | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus | |
| Mg2+ | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus | |
| SDS | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus | |
| K+ | 100 mM, decreases the rate of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin 2fold | Rattus norvegicus | |
| Mg2+ | significantly stimulates activity of the 20S proteasome at pH 7.5, completely inhibits at pH 5.5 | Rattus norvegicus | |
| Na+ | 100 mM, decreases the rate of hydrolysis of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin 2fold | Rattus norvegicus | |
| Zn2+ | does not significantly affect the activity of 20S proteasome at pH 7.5, the 20S proteasome expresses lower activity in the presence of Zn2+ ions in solution at the acidic pH | Rattus norvegicus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| natural killer cell | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | maximal chymotrypsin-like activity of the 20S proteasome, which contributes to the cytolytic mechanism of the natural killer cells, is associated with the conformational changes occuring in a cluster of highly conserved proteasome residues from the alpha-subunit that lead to the proteasome open conformation, allowing substrate access into the proteolytic chamber | Rattus norvegicus | ? | - |
? | |
| succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O | - |
Rattus norvegicus | ? | - |
? | |
| succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O | - |
Rattus norvegicus | ? | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
optimal cleavage of succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin | Rattus norvegicus |
| 7.5 | - |
optimal cleavage of succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin | Rattus norvegicus |
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