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Chemical Compound Review

actinonin     (2R)-N'-hydroxy-N-[(2S)-1- [(2S)-2...

Synonyms: Actinonine, CHEMBL308333, BSPBio_002379, KBioGR_002305, CCG-38543, ...
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Disease relevance of Actinonine


High impact information on Actinonine

  • We designed and synthesized 33 chemical analogs of actinonin; all of the molecules with potent activity against HsPDF also inhibited tumor cell growth, and vice versa, confirming target specificity [6].
  • We show that actinonin, a peptidomimetic antibiotic that inhibits HsPDF, also inhibits the proliferation of 16 human cancer cell lines [6].
  • Actinonin treatment of cells led to a tumor-specific mitochondrial membrane depolarization and ATP depletion in a time- and dose-dependent manner; removal of actinonin led to a recovery of the membrane potential consistent with indirect effects on the electron transport chain [6].
  • Disruption of PDF1B in A.thaliana led to an albino phenotype, and an extreme sensitivity to the PDF- specific inhibitor actinonin [7].
  • Actinonin, the most potent N-aminopeptidase inhibitor, was used to engage CD13 on sorted CD13(hi)Lin- cells and on culture day-7 bulk cells [8].

Chemical compound and disease context of Actinonine


Biological context of Actinonine


Anatomical context of Actinonine


Associations of Actinonine with other chemical compounds

  • Other cytosolic neutral aminopeptidase inhibitors such as actinonin and puromycin also augmented cell growth suppression by CH11, while an enantiomer of bestatin lacking aminopeptidase inhibitory action did not increase the growth-inhibitory effects of CH11 [17].
  • Renal slices are protected from hypoxia-reoxygenation injury in vitro by the meprin inhibitor actinonin [18].
  • Pre-treatment with the actinonin was markedly protective while not interfering with the hypoxia-induced fall in adenosine 5'-triphosphate (ATP) levels [18].
  • To identify novel PDF inhibitors, we screened a metalloenzyme inhibitor library and identified an N-formyl-hydroxylamine derivative, BB-3497, and a related natural hydroxamic acid antibiotic, actinonin, as potent and selective inhibitors of PDF [19].
  • This induction-dependent increase of GSK-3beta is markedly reduced in response to inhibitors of alanyl-aminopeptidase, actinonin, leuhistin, and RB3014 [20].

Gene context of Actinonine


Analytical, diagnostic and therapeutic context of Actinonine


  1. Reducing the fitness cost of antibiotic resistance by amplification of initiator tRNA genes. Nilsson, A.I., Zorzet, A., Kanth, A., Dahlström, S., Berg, O.G., Andersson, D.I. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure. Solbiati, J., Chapman-Smith, A., Cronan, J.E. J. Biol. Chem. (2002) [Pubmed]
  3. Antitumor activity of actinonin in vitro and in vivo. Xu, Y., Lai, L.T., Gabrilove, J.L., Scheinberg, D.A. Clin. Cancer Res. (1998) [Pubmed]
  4. The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents. Guilloteau, J.P., Mathieu, M., Giglione, C., Blanc, V., Dupuy, A., Chevrier, M., Gil, P., Famechon, A., Meinnel, T., Mikol, V. J. Mol. Biol. (2002) [Pubmed]
  5. Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis. Dirk, L.M., Williams, M.A., Houtz, R.L. Plant Physiol. (2001) [Pubmed]
  6. Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics. Lee, M.D., She, Y., Soskis, M.J., Borella, C.P., Gardner, J.R., Hayes, P.A., Dy, B.M., Heaney, M.L., Philips, M.R., Bornmann, W.G., Sirotnak, F.M., Scheinberg, D.A. J. Clin. Invest. (2004) [Pubmed]
  7. Control of protein life-span by N-terminal methionine excision. Giglione, C., Vallon, O., Meinnel, T. EMBO J. (2003) [Pubmed]
  8. CD13/N-aminopeptidase is involved in the development of dendritic cells and macrophages from cord blood CD34(+) cells. Rosenzwajg, M., Tailleux, L., Gluckman, J.C. Blood (2000) [Pubmed]
  9. Potent homophthalimide-type inhibitors of B16F10/L5 mouse melanoma cell invasion. Kagechika, H., Komoda, M., Fujimoto, Y., Koiso, Y., Takayama, H., Kadoya, S., Miyata, K., Kato, F., Kato, M., Hashimoto, Y. Biol. Pharm. Bull. (1999) [Pubmed]
  10. The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction. Brooks, D.R., Hooper, N.M., Isaac, R.E. J. Biol. Chem. (2003) [Pubmed]
  11. Endostatin binds to the catalytic domain of matrix metalloproteinase-2. Lee, S.J., Jang, J.W., Kim, Y.M., Lee, H.I., Jeon, J.Y., Kwon, Y.G., Lee, S.T. FEBS Lett. (2002) [Pubmed]
  12. Inhibition of alanyl aminopeptidase induces MAP-kinase p42/ERK2 in the human T cell line KARPAS-299. Lendeckel, U., Kähne, T., Arndt, M., Frank, K., Ansorge, S. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  13. Subinhibitory concentrations of the deformylase inhibitor actinonin increase bacterial release of neutrophil-activating peptides: a new approach to antimicrobial chemotherapy. Fu, H., Dahlgren, C., Bylund, J. Antimicrob. Agents Chemother. (2003) [Pubmed]
  14. Identification of extra- and intracellular alanyl aminopeptidases as new targets to modulate keratinocyte growth and differentiation. Thielitz, A., Bukowska, A., Wolke, C., Vetter, R., Lendeckel, U., Wrenger, S., Hashimoto, Y., Ansorge, S., Gollnick, H., Reinhold, D. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  15. Composite effects of actinonin when inhibiting enkephalin-degrading enzymes. Hachisu, M., Hiranuma, T., Shibazaki, Y., Uotani, K., Murata, S., Aoyagi, T., Umezawa, H. Eur. J. Pharmacol. (1987) [Pubmed]
  16. Aminopeptidase inhibitors inhibit proliferation and induce apoptosis of K562 and STI571-resistant K562 cell lines through the MAPK and GSK-3beta pathways. Sawafuji, K., Miyakawa, Y., Weisberg, E., Griffin, J.D., Ikeda, Y., Kizaki, M. Leuk. Lymphoma (2003) [Pubmed]
  17. Augmentation of death ligand-induced apoptosis by aminopeptidase inhibitors in human solid tumor cell lines. Sekine, K., Fujii, H., Abe, F., Nishikawa, K. Int. J. Cancer (2001) [Pubmed]
  18. Meprin, a brush-border enzyme, plays an important role in hypoxic/ischemic acute renal tubular injury in rats. Carmago, S., Shah, S.V., Walker, P.D. Kidney Int. (2002) [Pubmed]
  19. Antibiotic activity and characterization of BB-3497, a novel peptide deformylase inhibitor. Clements, J.M., Beckett, R.P., Brown, A., Catlin, G., Lobell, M., Palan, S., Thomas, W., Whittaker, M., Wood, S., Salama, S., Baker, P.J., Rodgers, H.F., Barynin, V., Rice, D.W., Hunter, M.G. Antimicrob. Agents Chemother. (2001) [Pubmed]
  20. Inhibition of alanyl-aminopeptidase suppresses the activation-dependent induction of glycogen synthase kinase-3beta (GSK-3beta) in human T cells. Lendeckel, U., Scholz, B., Arndt, M., Frank, K., Spiess, A., Chen, H., Roques, B.P., Ansorge, S. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  21. Enhancement of sensitivity by bestatin of acute promyelocytic leukemia NB4 cells to all-trans retinoic acid. Hirano, T., Kizaki, M., Kato, K., Abe, F., Masuda, N., Umezawa, K. Leuk. Res. (2002) [Pubmed]
  22. Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor. Chen, D.Z., Patel, D.V., Hackbarth, C.J., Wang, W., Dreyer, G., Young, D.C., Margolis, P.S., Wu, C., Ni, Z.J., Trias, J., White, R.J., Yuan, Z. Biochemistry (2000) [Pubmed]
  23. Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene. Margolis, P.S., Hackbarth, C.J., Young, D.C., Wang, W., Chen, D., Yuan, Z., White, R., Trias, J. Antimicrob. Agents Chemother. (2000) [Pubmed]
  24. Mechanism of time-dependent inhibition of polypeptide deformylase by actinonin. Van Aller, G.S., Nandigama, R., Petit, C.M., DeWolf, W.E., Quinn, C.J., Aubart, K.M., Zalacain, M., Christensen, S.B., Copeland, R.A., Lai, Z. Biochemistry (2005) [Pubmed]
  25. Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae. Chan, P.F., O'Dwyer, K.M., Palmer, L.M., Ambrad, J.D., Ingraham, K.A., So, C., Lonetto, M.A., Biswas, S., Rosenberg, M., Holmes, D.J., Zalacain, M. J. Bacteriol. (2003) [Pubmed]
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