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Literature summary for 3.4.21.12 extracted from
- The 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain (2004), J. Mol. Biol., 338, 999-1013.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure solved at 0.83 A resolution at pH 8 | Lysobacter enzymogenes |
General Stability
| General Stability | Organism |
|---|---|
| kinetic stability impaired by the large, cooperative unfolding barrier plays a critical role in extending the lifetime of the protease in its harsh environment | Lysobacter enzymogenes |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Lysobacter enzymogenes | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lysobacter enzymogenes | P00778 | - |
- |
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Release 2023.1 (January 2023)
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