The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Piericidin     2-[(2E,5E,7E,9R,10R,11E)-10- hydroxy-3,7,9...

Synonyms: Shaoguamycin B, Piericidine A, Piericidin A, Piericidin A1, CHEMBL272733, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Piericidin A

  • Piericidin-resistant mutants of the bacterium Rhodobacter capsulatus have been isolated and the present work demonstrates that a single missense mutation at the level of the gene encoding the peripheral 49-kDa/NUOD subunit of Complex I is definitely associated with this resistance [1].
  • IT-143-A and B, novel piericidin-group antibiotics produced by Streptomyces sp [2].
  • Acute toxicities of these substances in mice were lower than that of piericidin A1 [3].
  • In the course of a screening program for inhibitors of epidermal growth factor (EGF)-induced phosphatidylinositol turnover in human epidermoid carcinoma cell line A431, we discovered two novel compounds of the piericidin family from the culture broth and mycelia of a Streptomyces strain MJ288-OF3 [4].

High impact information on Piericidin A

  • Piericidin A sensitive delta psi formation has been demonstrated to be coupled to the NADH-MQ1 oxidoreductase in membrane vesicles of T. thermophilus HB-8 [5].
  • MPP+ and its analogues have been shown to block electron transport at or near the same site as two powerful inhibitors of mitochondrial respiration, rotenone and piericidin A [6].
  • The lesser protection by the more lipophilic MPP+ analogs with longer alkyl chains may involve a different orientation in the hydrophobic cleft, allowing rotenone and piericidin to still bind even when the pyridinium cation is in a position to interrupt electron flow from NADH to coenzyme Q [7].
  • Based on this original observation, we propose a model locating the binding site for piericidin (and quinone) at the interface between the hydrophilic and hydrophobic domains of Complex I [1].
  • Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+ [8].

Biological context of Piericidin A


Anatomical context of Piericidin A


Associations of Piericidin A with other chemical compounds


Analytical, diagnostic and therapeutic context of Piericidin A

  • In P. denitrificans, the forward and reverse reactions show different sensitivity to piericidin and the titrations of both activities were curvilinear with apparent I(50) (expressed as mole of inhibitor per mole of enzyme) independent of the enzyme concentration [15].


  1. The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors. Darrouzet, E., Issartel, J.P., Lunardi, J., Dupuis, A. FEBS Lett. (1998) [Pubmed]
  2. IT-143-A and B, novel piericidin-group antibiotics produced by Streptomyces sp. Urakawa, A., Sasaki, T., Yoshida, K., Otani, T., Lei, Y., Yun, W. J. Antibiot. (1996) [Pubmed]
  3. New piericidin glucosides, glucopiericidins A and B. Matsumoto, M., Mogi, K., Nagaoka, K., Ishizeki, S., Kawahara, R., Nakashima, T. J. Antibiot. (1987) [Pubmed]
  4. Isolation and structure determination of novel phosphatidylinositol turnover inhibitors, piericidin B5 and B5 N-oxide, from Streptomyces sp. Nishioka, H., Sawa, T., Takahashi, Y., Naganawa, H., Hamada, M., Takeuchi, T., Umezawa, K. J. Antibiot. (1993) [Pubmed]
  5. Studies on the NADH-menaquinone oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8. Meinhardt, S.W., Wang, D.C., Hon-nami, K., Yagi, T., Oshima, T., Ohnishi, T. J. Biol. Chem. (1990) [Pubmed]
  6. Reactivation of NADH dehydrogenase (complex I) inhibited by 1-methyl-4-(4'-alkylphenyl)pyridinium analogues: a clue to the nature of the inhibition site. Krueger, M.J., Sablin, S.O., Ramsay, R., Singer, T.P. J. Neurochem. (1993) [Pubmed]
  7. Interaction of 1-methyl-4-phenylpyridinium ion (MPP+) and its analogs with the rotenone/piericidin binding site of NADH dehydrogenase. Ramsay, R.R., Krueger, M.J., Youngster, S.K., Gluck, M.R., Casida, J.E., Singer, T.P. J. Neurochem. (1991) [Pubmed]
  8. Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+. Ramsay, R.R., Singer, T.P. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  9. Effect of oxidative stress on dynamics of mitochondrial reticulum. Pletjushkina, O.Y., Lyamzaev, K.G., Popova, E.N., Nepryakhina, O.K., Ivanova, O.Y., Domnina, L.V., Chernyak, B.V., Skulachev, V.P. Biochim. Biophys. Acta (2006) [Pubmed]
  10. Evidence that the inhibition sites of the neurotoxic amine 1-methyl-4-phenylpyridinium (MPP+) and of the respiratory chain inhibitor piericidin A are the same. Ramsay, R.R., Krueger, M.J., Youngster, S.K., Singer, T.P. Biochem. J. (1991) [Pubmed]
  11. Effect of inhibitors on the substrate-dependent quenching of 9-aminoacridine fluorescence in inside-out membrane vesicles of Escherichia coli. Singh, A.P., Bragg, P.D. Eur. J. Biochem. (1976) [Pubmed]
  12. Pharmacological properties of melochinine, an alkaloid producing Central American cattle paralysis. Breuer, H., Rangel, M., Medina, E. Toxicology (1982) [Pubmed]
  13. Production of reactive oxygen species in mitochondria of HeLa cells under oxidative stress. Chernyak, B.V., Izyumov, D.S., Lyamzaev, K.G., Pashkovskaya, A.A., Pletjushkina, O.Y., Antonenko, Y.N., Sakharov, D.V., Wirtz, K.W., Skulachev, V.P. Biochim. Biophys. Acta (2006) [Pubmed]
  14. New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles. van Belzen, R., van Gaalen, M.C., Cuypers, P.A., Albracht, S.P. Biochim. Biophys. Acta (1990) [Pubmed]
  15. The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites. Grivennikova, V.G., Roth, R., Zakharova, N.V., Hägerhäll, C., Vinogradov, A.D. Biochim. Biophys. Acta (2003) [Pubmed]
WikiGenes - Universities