Primary information |
---|
ID | antitb_1013 |
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 smegmatis |
Strain | Mycobacterium smegmatis (ATCC 700084) |
Inhibition Concentartion | MIC = 1.7 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 |