EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.92 | cyclomarin | cyclomarin binding to subunit ClpC1 N-terminal domain specifically blockes the N-terminal dynamics induced by arginine-phosphate binding. Cyclomarin-induced restriction of ClpC1 dynamics may modulate the chaperone enzymatic activity leading eventually to cell death | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.92 | Mycobacterium tuberculosis | - |
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EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.21.92 | physiological function | arginine-phosphate and arginine-phosphorylated proteins bind to subunit ClpC1 N-terminal domain and induce millisecond dynamics. These dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain | Mycobacterium tuberculosis |