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Literature summary extracted from
- Ubiquitination and proteasomal degrdn. of endogenous and exogenous inositol 1,4,5-trisphosphate receptors in aT3-1 anterior pituitary cells (2003), J. Biol. Chem., 278, 940-947.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.25.1 | additional information | occupancy of the caspase-like sites stimulates the trypsin-like activity of the proteasomes | Saccharomyces cerevisiae | |
| 3.4.25.1 | additional information | occupancy of the caspase-like sites stimulates the trypsin-like activity of the proteasomes | Oryctolagus cuniculus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.25.1 | acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde | 99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amido-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 89% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 24% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin | Oryctolagus cuniculus |  |
| 3.4.25.1 | acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde | - |
Saccharomyces cerevisiae | |
| 3.4.25.1 | AEBSF | 25% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, 22% inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 19% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 21% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 26% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, 98% inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amino-4-methylcoumarin | Oryctolagus cuniculus | |
| 3.4.25.1 | benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde | 99% inhibition of hydrolysis of acetyl-norleucine-Leu-Pro-norleucine-Leu-Asp-7-amino-4-methylcoumarin, complete inhibition of hydrolysis of acetyl-norleucine-GPLD-7-amido-4-methylcoumarin, 95% inhibition of hydrolysis of acetyl-GPLL-7-amido-4-methylcoumarin, 91% inhibition of hydrolysis of acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin, 12% inhibition of hydrolysis of succinyl-LLVY-7-amido-4-methylcoumarin, no inhibition of hydrolysis of tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin | Oryctolagus cuniculus | |
| 3.4.25.1 | benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde | - |
Saccharomyces cerevisiae | |
| 3.4.25.1 | additional information | although inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity, inhibitors of the caspase-like sites allosterically inhibit the chymotrypsin-like activity. When caspase-like sites are occupied by the uncleaved propeptide or inhibitor, their substrates still inhibit the chymotrypsin like activity | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.25.1 | additional information | Oryctolagus cuniculus | proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.25.1 | Oryctolagus cuniculus | - |
- |
- |
| 3.4.25.1 | Saccharomyces cerevisiae | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.25.1 | muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.25.1 | acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLD-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-GPLD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLD-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-GPLD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLE-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-GPLE + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLE-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-GPLE + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLL-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-GPLL + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-GPLL-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-GPLL + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-YVAD-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | acetyl-YVAD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | acetyl-YVAD-7-amido-4-methylcoumarin + H2O | - |
Oryctolagus cuniculus | acetyl-YVAD + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.1 | additional information | proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Caspase-like sites cleave after aspartates better than after glutamates | Oryctolagus cuniculus | ? | - |
? | |
| 3.4.25.1 | additional information | proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites | Oryctolagus cuniculus | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.25.1 | 20S proteasome | - |
Saccharomyces cerevisiae |
| 3.4.25.1 | 26S proteasome | - |
Oryctolagus cuniculus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.25.1 | additional information | - |
additional information | - |
Oryctolagus cuniculus | |
| 3.4.25.1 | 0.02 | - |
acetyl-Ala-Pro-norleucine-Leu-Asp-aldehyde | - |
Saccharomyces cerevisiae | |
| 3.4.25.1 | 0.021 | - |
benzyloxycarbonyl-Pro-norleucine-Leu-Asp-aldehyde | - |
Saccharomyces cerevisiae | |
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