Further studies on ASN-136 and monoketo-organomycin cystaurimycin, a broad spectrum substance produced by partial enzymic digestion of monoketo-organomycin.

@article{Imam1977FurtherSO,
  title={Further studies on ASN-136 and monoketo-organomycin cystaurimycin, a broad spectrum substance produced by partial enzymic digestion of monoketo-organomycin.},
  author={Gamal M. Imam and Hans Küntzel},
  journal={The Journal of antibiotics},
  year={1977},
  volume={30 4},
  pages={
          314-20
        }
}
The two antibiotics ASN-136 and monoketo-organomycin (MKOM) showed very close similarities in their UV, IR spectra and elemental analysis to those of tuberactinomycin and yazumycin respectively. Further chemical and enzymic studies revealed the novelty of the two former antibiotics. Partial enzymic hydrolysis of MKOM yielded a hydrolytic product of more potent inhibitory action compared with the parent antibiotic. Having cystine as the N-terminus and taurine as the C-terminus in its molecule… 
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Mechanism of action of monoketo-organomycin, cystaurimycin and their performic acid-oxidized modifications. II. Inhibition of mitochondrial ATPase activity in Aspergillus nidulans and identification of the performic acid-oxidized modifications-binding protein.

  • G. Imam
  • Biology, Chemistry
    The Journal of antibiotics
  • 1979
Performic acid-oxidized modifications of monoketo-organomycin and cystaurimycin1) were found to possess identical mechanisms of action. Both inhibit mitochondrial ATPase activity in Aspergillus

Mechanism of action of monoketo-organomycin, cystaurimycin and their performic acid-oxidized modifications. I. Effects on bacterial growth and ribosomal peptidyl transferase activity.

In light of the puromycin reaction, using chloramphenicol and chlorotetracycline as control inhibitors, monoketo-organomycin and cystaurimycin were found to inhibit protein synthesis in vitro by inhibiting peptidyl transferase of ribosomes.

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