| Primary information |
|---|
| ID | antitb_1015 |
| Peptide Name | Ecumicin |
| Sequence | (N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val) |
| N-terminal Modification | Free |
| C-terminal Modification | Free |
| Chemical Modification | N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe |
| Linear/ Cyclic | Macrocyclic |
| Length | 13 |
| Chirality | L |
| Nature | NA |
| Source | Natural |
| Origin | Produced by a genetically distinct Nonomuraea species, strain MJM5123. |
| Species | Mycobacterium marinum |
| Strain | Mycobacterium marinum (ATCC 927) |
| Inhibition Concentartion | MIC = 0.95 μM |
| In vitro/In vivo | In vitro |
| Cell Line | None |
| Inhibition Concentartion | NA |
| Cytotoxicity | NA |
| In vivo Model | None |
| Lethal Dose | None |
| Immune Response | NA |
| Mechanism of Action | Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin |
| Target | ClpC1 ATPase complex |
| Combination Therapy | None |
| Other Activities | NA |
| Pubmed ID | 25421483 |
| Year of Publication | 2015 |
| 3-D Structure | NA |