Open AccessThe Photochemical Inactivation of Peptidyl Transferase Activity
Author(s) -
WAN Kwong K.,
ZAHID Nasir D.,
BAXTER Ross M.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02386.x
Subject(s) - chemistry , transferase , peptidyl transferase , photochemistry , biophysics , biology , biochemistry , enzyme , gene , ribosome , rna
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 inactivated. The pH profile of inactivation exhibits a maximum at pH 7.5. Erythromycin at a low concentration (0.04 μmol) 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.