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Chemical Compound Review

Mucidin     methyl(2E,3Z,5E)-2- (methoxymethylidene)-3...

Synonyms: OM-1, AmbotzLS-1154, AC1O5NKA, LS-93712, 52110-55-1
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Disease relevance of Mucidin


High impact information on Mucidin


Chemical compound and disease context of Mucidin

  • A new method of determination of nitrate was developed, utilizing the nitrate reductase activity of Paracoccus denitrificans in which a further reduction of nitrate is blocked either by a mutation affecting formation of cytochromes c or by inhibition of the electron flow to nitrite reductase by mucidin [4].

Biological context of Mucidin

  • Mucidin and strobilurin A, antifungal antibiotics isolated from the basidiomycetes Oudemansiella mucida and Strobiluris tenacellus, respectively, inhibit electron-transfer reactions in the cytochrome bc1 complex of the mitochondrial respiratory chain [5].
  • Resistance to mucidin in class 1 mutants was due to a single-gene nuclear recessive mutation (mucPR) whereas that in class 2 mutants was caused by mutations of mitochondrial genes [6].
  • Allelism tests indicated that the mucidin resistance mutations fell into two genetic loci (MUC1 and MUC2) which were apparently not closely linked in the mitochondrial genome [6].
  • It is concluded that the extra reduction of cytochrome b-565 and the red shift of cytochrome b-561 elicited by mucidin can be largely dissociated from the overall inhibition of the electron flow by distinct mucidin-resistant mutations in different exons of the split mitochondrial gene of cytochrome b [7].
  • Genetic mapping of nuclear mucidin resistance mutations in Saccharomyces cerevisiae. A new pdr locus on chromosome II [8].

Anatomical context of Mucidin


Associations of Mucidin with other chemical compounds


Gene context of Mucidin

  • These effects of mucidin and strobilurin A are, however, qualitatively identical with those of myxothiazol, an antibiotic that inhibits respiration by binding to cytochrome b [Von Jagow, G., Ljungdahl, P. O., Graf, P., Ohnishi, T., & Trumpower, B. L. (1984) J. Biol. Chem. 259, 6319-6326] [5].
  • Mutants of Saccharomyces cerevisiae resistant to the antibiotic mucidin, a specific inhibitor of electron transport between cytochrome b and c, were isolated and divided into three phenotypic groups, as follows [6].
  • Recombination studies showed that the two mitochondrial mucidin loci were not allelic with other mitochondrial loci RIB1, RIB2 and OLI1 [6].

Analytical, diagnostic and therapeutic context of Mucidin


  1. Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrificans bacteria. Kucera, I., Hedbávný, R., Dadák, V. Biochem. J. (1988) [Pubmed]
  2. Molecular basis for resistance to myxothiazol, mucidin (strobilurin A), and stigmatellin. Cytochrome b inhibitors acting at the center o of the mitochondrial ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae. di Rago, J.P., Coppée, J.Y., Colson, A.M. J. Biol. Chem. (1989) [Pubmed]
  3. Role of the PDR gene network in yeast susceptibility to the antifungal antibiotic mucidin. Michalkova-Papajova, D., Obernauerova, M., Subik, J. Antimicrob. Agents Chemother. (2000) [Pubmed]
  4. Determination of nitrate by conversion to nitrite using Paracoccus denitrificans. Matchová, I., Cerná, I., Kucera, I. Folia Microbiol. (Praha) (1991) [Pubmed]
  5. Mucidin and strobilurin A are identical and inhibit electron transfer in the cytochrome bc1 complex of the mitochondrial respiratory chain at the same site as myxothiazol. Von Jagow, G., Gribble, G.W., Trumpower, B.L. Biochemistry (1986) [Pubmed]
  6. Mucidin resistance in yeast. Isolation, characterization and genetic analysis of nuclear and mitochondrial mucidin-resistant mutants of Saccharomyces cerevisiae. Subík, J., Kovácová, V., Takáscová, G. Eur. J. Biochem. (1977) [Pubmed]
  7. Spectral properties of cytochrome b-561 and cytochrome b-565 in mucidin-resistant mutants of Saccharomyces cerevisiae. Subík, J., Briquet, M., Goffeau, A. Eur. J. Biochem. (1981) [Pubmed]
  8. Genetic mapping of nuclear mucidin resistance mutations in Saccharomyces cerevisiae. A new pdr locus on chromosome II. Subik, J., Ulaszewski, S., Goffeau, A. Curr. Genet. (1986) [Pubmed]
  9. Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain. Ksenzenko, M., Konstantinov, A.A., Khomutov, G.B., Tikhonov, A.N., Ruuge, E.K. FEBS Lett. (1983) [Pubmed]
  10. Genetic localization of diuron- and mucidin-resistant mutants relative to a group of loci of the mitochondrial DNA controlling coenzyme QH2-cytochrome c reductase in Saccharomyces cerevisiae. Colson, A.M., Slonimski, P.P. Mol. Gen. Genet. (1979) [Pubmed]
  11. Isolation and molecular characterization of the carboxy-terminal pdr3 mutants in Saccharomyces cerevisiae. Simonics, T., Kozovska, Z., Michalkova-Papajova, D., Delahodde, A., Jacq, C., Subik, J. Curr. Genet. (2000) [Pubmed]
  12. Study of Trichoderma viride metabolism under conditions of the restriction of oxidative processes. Chovanec, P., Kalinák, M., Liptaj, T., Pronayová, N., Jakubík, T., Hudecová, D., Varecka, L. Can. J. Microbiol. (2005) [Pubmed]
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