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Literature summary extracted from
- The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic dyad of Lon proteases (2004), J. Biol. Chem., 279, 53451-53457.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | contains two transmembrane helices within its N-terminal domain | Methanocaldococcus jannaschii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | Methanocaldococcus jannaschii | - |
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- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.21.53 | hydrolysis of proteins in presence of ATP | active site consists of catalytic Ser-Lys-Asp residues. Charged Lys-593 assists in lowering the pKa of the Ser550 hydroxyl group, and the water in the cavity acts as a proton acceptor during catalysis | Methanocaldococcus jannaschii |
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Release 2023.1 (January 2023)
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