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Literature summary for 3.4.25.1 extracted from
- Proteasomal activities in the claw muscle tissue of European lobster, Homarus gammarus, during larval development (2011), J. Comp. Physiol. B, 181, 861-871.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| epoxomicin | inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview | Homarus gammarus |  |
| PA28 | inhibition of the protease activities of the of the 20S- and 26S proteasome in all larvaeal stages, overview | Homarus gammarus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homarus gammarus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| claw muscle | trypsin-like, the chymotrypsin-like, and the peptidyl-glutamyl peptide hydrolase activity of the 20S proteasome increase distinctly from freshly hatched larvae to pre-molt Z1. During the Z2 stage, the activities are highest in the post-molt animals, decrease in the inter-molt animals, and increase again in the pre-molt animals. A similar but less distinct trend is evident in the Z3 stages. In the juveniles, the proteasomal activities decrease toward the lowest values. A similar pattern is present for the chymotrypsin-like activity of the 26S proteasome | Homarus gammarus | - |
| larva | of all three zoea stages Z1-Z3, as well as the first juvenile stage J1 | Homarus gammarus | - |
| additional information | not in gastric fluid | Homarus gammarus | - |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homarus gammarus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homarus gammarus |
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