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Literature summary extracted from
- A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization (2013), J. Biol. Chem., 288, 17884-17894.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | expression in Escherichia coli | Pyrococcus horikoshii |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | crystals are grown at 20°C by the hanging drop method | Pyrococcus horikoshii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | Pyrococcus horikoshii | O58323 | - |
- |
| 3.4.19.1 | Pyrococcus horikoshii DSM 12428 | O58323 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | - |
Pyrococcus horikoshii |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | hexamer | hexamers in the crystalline state are formed as trimers of dimers of the monomer enzyme. It is proposed that the mode of multimerization and self-assembly among oligopeptidases is finetuned by a shielding intent of a sticky-edge, insertions, and N- and C-terminal extensions, whereas to maintain the effectiveness of catalysis and selectivity, pliability of the His-loop and the position of the propeller blades are adjusted | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | PhAAP | - |
Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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