Protein Variants | Comment | Organism |
---|---|---|
G166R | the mutant is both more stable and displays more activity compared to the wild-type enzyme | Bacillus licheniformis |
S161C | the mutant brings increased stability to subtilisin compared to the wild-type | Bacillus licheniformis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | molecular dynamics simulations, residue displacement correlations, and inhibitor design based on the enzyme inhibitor comlpex of TI-II and subtilisin, overview | Bacillus licheniformis | |
tomato inhibitor-II | TI-II, enzyme binding structure, the interdomain interface in TI-II consists of a small cluster of highly conserved hydrophobic residues Ile14, Pro16, Tyr98, Phe100 and Phe106 from domain I and Tyr34, Pro54 and Lys55 from domain II. Although this interface is quite small (buried surface area of 487A), it forms a stable packing arrangement between the two domains. Each reactive site loop in TI-II interacts with a separate molecule of subtilisin in the canonical manner observed in other proteinaseinhibitor complexes. The domains of TI-II appear to bind the proteinase independently of each other | Bacillus licheniformis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
subtilisin Carlsberg | - |
Bacillus licheniformis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Bacillus licheniformis |