Metabolites-BOC Sciences


Actinonin - CAS 13434-13-4

Catalog number: BBF-00543

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Catalog Number BBF-00543
CAS 13434-13-4
Description Actinonin, a natural antibacterial agent produced by Actinomyces, is a potent reversible peptide deformylase (PDF) inhibitor with Ki of 0.28 nM. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin induces apoptosis and has antiproliferative and antitumor activities..
Molecular Formula C19H35N3O5
Molecular Weight 385.51
Antibiotic Activity Spectrum Gram-positive bacteria; mycobacteria
Synonyms 3-[[1-[(2-(Hydroxymethyl)-1-pyrrolidinyl)carbonyl]-2-methylpropyl]carbamoyl]octanohydroxamic acid
IUPAC Name N'-hydroxy-N-[1-[2-(hydroxymethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]-2-pentylbutanediamide
InChI InChI=1S/C19H35N3O5/c1-4-5-6-8-14(11-16(24)21-27)18(25)20-17(13(2)3)19(26)22-10-7-9-15(22)12-23/h13-15,17,23,27H,4-12H2,1-3H3,(H,20,25)(H,21,24)
Melting Point 137-139°C
Purity ≥98% by TLC
Density 1.139 g/cm3
Appearance Colorless Needle Crystal
Storage Store at -20°C
1.Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.
Ganji RJ1, Reddi R, Gumpena R, Marapaka AK, Arya T, Sankoju P, Bhukya S, Addlagatta A. Protein Sci. 2015 May;24(5):823-31. doi: 10.1002/pro.2653. Epub 2015 Apr 8.
Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the major differences in terms of substrate binding pockets between these families is presence (in M1 aminopeptidases) or absence (in PDFs) of an S1 substrate pocket. The binding mode of actinonin to PDFs has been established previously; however, it is not clear how the actinonin, without a P1 residue, would bind to the M1 aminopeptidases. Here we describe the crystal structure of Escherichia coli aminopeptidase N (ePepN), a model protein of the M1 family aminopeptidases in complex with actinonin. For comparison we have also determined the structure of ePepN in complex with a well-known tetrapeptide inhibitor, amastatin. From the comparison of the actinonin and amastatin ePepN complexes, it is clear that the P1 residue is not critical as long as strong metal chelating head groups, like hydroxamic acid or α-hydroxy ketone, are present.
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