Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Bovine glucagon | activation, glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP, not casein hydrolysis | Escherichia coli | |
casein | activation, glutaryl-Ala-Ala-Phe-methoxynaphthylamide or insulin B-chain hydrolysis, in the absence of ATP and synergistic with ATP | Escherichia coli | |
Denatured bovine serum albumin | activation | Escherichia coli | |
Denatured bovine serum albumin | glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP | Escherichia coli | |
Denatured immunoglobin G | activation | Escherichia coli | |
Denatured immunoglobin G | peptide hydrolysis, with or without ATP | Escherichia coli | |
Globin | activation, peptide hydrolysis | Escherichia coli | |
additional information | no activation by nonhydrolyzable proteins, e.g. native or denatured ribonuclease or lysozyme | Escherichia coli | |
Protein substrates | activation | Escherichia coli | |
Protein substrates | rise in ATPase activity proportional to peptide bonds cleaved | Escherichia coli | |
Protein substrates | protein substrates enhance additively the stimulating effect of ATP on peptide hydrolysis and even in the absence of ATP they enhance the ability to degrade fluorogenic tripeptides | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | casein (with peptides as substrates) | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.026 | - |
alpha-casein | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Proteins with highly abnormal conformation + H2O | Escherichia coli | rate-limiting step in breakdown of highly abnormal and some normal proteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | - |
Escherichia coli | ? | - |
? | |
Denatured bovine serum albumin + H2O | - |
Escherichia coli | ? | - |
? | |
Denatured immunoglobulin G + H2O | - |
Escherichia coli | ? | - |
? | |
Globin + H2O | - |
Escherichia coli | ? | - |
? | |
additional information | No substrates are native bovine serum albumin, hemoglobin | Escherichia coli | ? | - |
? | |
additional information | the active site prefers hydrophobic substrate sequences | Escherichia coli | ? | - |
? | |
additional information | No substrates are benzyloxycarbonyl-Ala-Arg-Arg-methoxynaphthylamide, native or denatured ribonuclease, native or denatured lysozyme, native immunoglobulin G | Escherichia coli | ? | - |
? | |
Proteins with highly abnormal conformation + H2O | rate-limiting step in breakdown of highly abnormal and some normal proteins | Escherichia coli | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP-dependent protease | Escherichia coli |