General Stability | Organism |
---|---|
alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities | Lysobacter enzymogenes |
lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity | Lysobacter enzymogenes |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity | Lysobacter enzymogenes |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lysobacter enzymogenes | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-Ala-Pro-Ala-4-nitroanilide + H2O | - |
Lysobacter enzymogenes | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alpha-lytic protease | - |
Lysobacter enzymogenes |