Literature DB >> 241639

The photochemical inactivation of peptidyl transferase activity.

K K Wan, N D Zahid, R M Baxter.   

Abstract

The photochemical oxidation of the 50-S ribosomal subunit results in a rapid irreversible loss of peptidyl transferase activity. The first-order rate of inactivation occurring during the first forty minutes suggests that a single reactive group is being inactivation exhibits a maximum at pH 7.5. Erythromycin at a low concentration (0.04 mumol) affords significant protection. Puromycin also exerts a protective effect but at higher concentrations. Chloramphenicol, sparsomycin and lincomycin did not exert a protective effect. The loss in catalytic activity was not accompanied by a loss in substrate binding affinity of the donor and acceptor substrates.

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Year:  1975        PMID: 241639     DOI: 10.1111/j.1432-1033.1975.tb02386.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer.

Authors:  G Diedrich; C M Spahn; U Stelzl; M A Schäfer; T Wooten; D E Bochkariov; B S Cooperman; R R Traut; K H Nierhaus
Journal:  EMBO J       Date:  2000-10-02       Impact factor: 11.598

2.  Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity.

Authors:  H Schulze; K H Nierhaus
Journal:  EMBO J       Date:  1982       Impact factor: 11.598

  2 in total

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