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PMID: 1225607 Published · ppublish English Journal Article

Effect of cytidine-5'-monophosphate on peptidyl transferase activity.

FEBS letters ·Vol. 58 ·No. 1 ·1975-10-15 ·Pages 94-8

Cerná J

Abstract

The transfer reaction with pA-fMet as a donor substrate is strongly stimulated by CMP, whereas the transfer reaction with CpApCpCpA-acLeu as a donor substrate is inhibited by CMP. These results indicate that the donor site of peptidyl transferase contains specific binding sites for the terminal adenosine and for the cytidylic acid residue in the terminal sequence CpCpA of tRNA and that an attachment of proper nucleotides to the donor site induces a conformational change in peptidyl transferase.

MeSH Terms
Acyltransferases/metabolism Adenine Nucleotides/metabolism Anti-Bacterial Agents/pharmacology Binding Sites Cytidine Monophosphate/pharmacology Cytosine Nucleotides/pharmacology Enzyme Activation N-Formylmethionine/metabolism Peptidyl Transferases/metabolism Protein Conformation/drug effects RNA, Transfer/metabolism Ribosomes/enzymology Structure-Activity Relationship
Chemicals
Adenine Nucleotides Anti-Bacterial Agents Cytosine Nucleotides N-Formylmethionine RNA, Transfer Acyltransferases Peptidyl Transferases Cytidine Monophosphate
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Cerná J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1975-10-15
Pages
94-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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