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Detailed description page of AntiTbPdb

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antitb_1015 details
Primary information
IDantitb_1015
Peptide NameEcumicin
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 ModificationFree
C-terminal ModificationFree
Chemical ModificationN-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/ CyclicMacrocyclic
Length13
ChiralityL
NatureNA
SourceNatural
OriginProduced by a genetically distinct Nonomuraea species, strain MJM5123.
SpeciesMycobacterium marinum
StrainMycobacterium marinum (ATCC 927)
Inhibition ConcentartionMIC = 0.95 μM
In vitro/In vivoIn vitro
Cell LineNone
Inhibition ConcentartionNA
CytotoxicityNA
In vivo ModelNone
Lethal DoseNone
Immune ResponseNA
Mechanism of ActionEcumicin 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
TargetClpC1 ATPase complex
Combination TherapyNone
Other ActivitiesNA
Pubmed ID25421483
Year of Publication2015
3-D StructureNA