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Literature summary for 3.4.21.92 extracted from
- Validation of the essential ClpP protease in Mycobacterium tuberculosis as a novel drug target (2012), J. Bacteriol., 194, 663-668.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| acyldepsipeptides | ADEP series 2, 3, 4 as well as two other synthesized derivatives, IDR-10001 and IDR-10011, which incorporate N-methylalanine instead of the more rigid homoproline in the depsipeptide core structure. All five compound are active against Mycobacterium tuberculosis, ADEP2 is the most active | Mycobacterium tuberculosis |
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | ClpP activation is an effective means of controlling the replication of Mycobacterium tuberculosis | Mycobacterium tuberculosis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
possesses two ClpP proteolytic subunits | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ClpP1 protease | - |
Mycobacterium tuberculosis |
| ClpP2 protease | - |
Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | ClpP1 is essential for viability. The gene can only be deleted from the chromosome when a second functional copy is provided. Over-expression of clpP1 has no effect on growth in aerobic culture or viability under anaerobic conditions or during nutrient starvation | Mycobacterium tuberculosis |
| malfunction | clpP2 over-expression is toxic | Mycobacterium tuberculosis |
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