Any feedback?
Literature summary extracted from
- Highly dynamic interactions maintain kinetic stability of the ClpXP protease during the ATP-fueled mechanical cycle (2016), ACS Chem. Biol., 11, 1552-1560.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.92 | Escherichia coli | P0A6G7 | - |
- |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.21.92 | physiological function | ClpXP protease consists of the ClpX hexamer and the ClpP peptidase. Small-molecule acyldepsipeptides such as ADEP-2B compete with the IGF loops of ClpX for ClpP-cleft binding and cause exceptionally rapid dissociation of otherwise stable ClpXP complexes, suggesting that the IGF-loop interactions with ClpP must be highly dynamic | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
