[Guanyl cyclase activity in the EF-T elongation factor of Escherichia coli].
Highly purified EF-Ts from E. coli does contain guanylate cyclase activity, which is absent from other purified transfer factors, such as EF-Tu and EF-G. Guanylate cyclase activity has been characterized by its sensitivity to inhibitors and substrate specificity. Although the physicochemical properties of guanylate cyclase are closely related to those of EF-Ts, it does not appear to be a contaminant of this transfer factor, but a specific enzyme. The possible role of guanylate cyclase in protein synthesis is discussed.
D001312:Aurintricarboxylic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006162:Guanylate Cyclase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010445:Peptide Elongation Factors / Q000302:isolation & purification
D010445:Peptide Elongation Factors; D001312:Aurintricarboxylic Acid; D006162:Guanylate Cyclase
Activité guanylate cyclase dans le facteur d'élongation EF-Ts d'Escherichia coli.