1993
DOI: 10.1021/bi00091a014
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Abstract: The inhibition of peptide bond formation by spiramycin was studied in an in vitro system derived from Escherichia coli. Peptide bonds are formed between puromycin (S) and Ac-Phe-tRNA, which is a component of complex C, i.e., of the [Ac-Phe-tRNA-70S ribosome-poly(U)] complex, according to the puromycin reaction: C+S (Ks)<==>CS (k3)==>C'+P [Synetos, D., & Coutsogeorgopoulos, C. (1987) Biochim. Biophys. Acta 923, 275-285]. It is shown that spiramycin (A) reacts with complex C and forms the spiramycin complex C*A,… Show more

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Cited by 23 publications
(36 citation statements)
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References 36 publications
(36 reference statements)
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“…Inhibition of Peptide Bond Formation by Spiramycin-In agreement with previous results obtained at 10 mM Mg 2ϩ (16), spiramycin inactivates complex C at 6 mM Mg 2ϩ , almost irreversibly. Each time the plot reaches a plateau, which progressively bends down with increasing drug concentrations (plots not shown).…”
Section: Inhibition Of Peptide Bond Formation At High Concentrations supporting
confidence: 90%
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“…Inhibition of Peptide Bond Formation by Spiramycin-In agreement with previous results obtained at 10 mM Mg 2ϩ (16), spiramycin inactivates complex C at 6 mM Mg 2ϩ , almost irreversibly. Each time the plot reaches a plateau, which progressively bends down with increasing drug concentrations (plots not shown).…”
Section: Inhibition Of Peptide Bond Formation At High Concentrations supporting
confidence: 90%
“…Inactivation of Complex C by Spiramycin-The reaction of complex C with spiramycin in the absence of puromycin was examined as described previously (16).…”
Section: ) Of K Obs and [S] Values To Equationmentioning
confidence: 99%
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“…When k Ϫ1 Ͼ Ͼ k 12 , the first binding step equilibrates much faster than the subsequent strong binding of the drug. Elimination of the fast variable (25) can then be used to simplify the slow binding step according to Reaction 2 (26).…”
Section: Quantitative Analysismentioning
confidence: 99%