EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.62 | EDTA | inactivates the enzyme at 0.01 mM, the enzyme protein becomes less structured and potentially monomeric. Removal of Ca2+ at sites close to the dimer interface and the S1 pocket are involved enzyme inhhibition by EDTA | Alkalihalobacillus clausii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.21.62 | intracellular | - |
Alkalihalobacillus clausii | 5622 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.62 | Ca2+ | is important for ISP activity through structural changes. The looped turn constituted by residues Ala180-Pro197 binds Ca2+. Removal of Ca2+ at sites close to the dimer interface and the S1 pocket are involved enzyme inhhibition by EDTA | Alkalihalobacillus clausii | |
3.4.21.62 | additional information | metal ions are not involved in the subtilisin catalytic mechanism but are an important structural element | Alkalihalobacillus clausii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.62 | Alkalihalobacillus clausii | D0AB41 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.62 | Ala-Ala-Pro-Leu-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Pro-Leu + 4-nitroaniline | - |
? | |
3.4.21.62 | Ala-Ala-Pro-Lys-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Pro-Lys + 4-nitroaniline | - |
? | |
3.4.21.62 | Ala-Ala-Pro-Met-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Pro-Met + 4-nitroaniline | - |
? | |
3.4.21.62 | Ala-Ala-Pro-Nle-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Pro-Nle + 4-nitroaniline | - |
? | |
3.4.21.62 | Ala-Ala-Pro-Phe-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
3.4.21.62 | Ala-Ala-Val-Ala-4-nitroanilide + H2O | low activity | Alkalihalobacillus clausii | Ala-Ala-Val-Ala + 4-nitroaniline | - |
? | |
3.4.21.62 | Bovine serum albumin + H2O | poor substrate in native form, but can be digested in heat-denatured form | Alkalihalobacillus clausii | ? | - |
? | |
3.4.21.62 | lactate dehydrogenase + H2O | poor substrate in native form, but can be digested in heat-denatured form | Alkalihalobacillus clausii | ? | - |
? | |
3.4.21.62 | malate dehydrogenase + H2O | poor substrate in native form, but can be digested in heat-denatured form | Alkalihalobacillus clausii | ? | - |
? | |
3.4.21.62 | additional information | substrate specificity, substrate docking simulations, overview. No activity with Ala-Ala-Pro-Glu-4-nitroanilide and Tyr-Val-Ala-Asp-4-nitroanilide. Substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. The enzyme unfolds under stress conditions. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms | Alkalihalobacillus clausii | ? | - |
? | |
3.4.21.62 | Phe-Ala-Ala-Phe-4-nitroanilide + H2O | highly preferred substrate | Alkalihalobacillus clausii | Phe-Ala-Ala-Phe + 4-nitroaniline | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.21.62 | dimer | - |
Alkalihalobacillus clausii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.62 | intracellular subtilisin protease | - |
Alkalihalobacillus clausii |
3.4.21.62 | ISP | - |
Alkalihalobacillus clausii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.21.62 | evolution | the enzyme belongs to a structurally distinct class of the subtilase family | Alkalihalobacillus clausii |
3.4.21.62 | additional information | substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets | Alkalihalobacillus clausii |
3.4.21.62 | physiological function | modeling of intracellular subtilisin protease regulation within the cell | Alkalihalobacillus clausii |