Cyclic AMP stimulates the protein tyrosine kinase activity of Acinetobacter calcoaceticus

Abstract The protein tyrosine kinase activity of Acinetobacter calcoaceticus was analyzed in vitro through the specific phosphorylation of an endogenous protein which is modified exclusively at tyrosine residues. A strong stimulation of this activity by cyclic AMP was observed. This finding represen...

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Veröffentlicht in:FEMS microbiology letters 1997-07, Vol.152 (2), p.333-337
Hauptverfasser: Grangeasse, Christophe, Vaganay, Elisabeth, Doublet, Patricia, Riberty, Mylène, Cozzone, Alain J, Duclos, Bertrand
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Sprache:eng
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Zusammenfassung:Abstract The protein tyrosine kinase activity of Acinetobacter calcoaceticus was analyzed in vitro through the specific phosphorylation of an endogenous protein which is modified exclusively at tyrosine residues. A strong stimulation of this activity by cyclic AMP was observed. This finding represents the first example of a protein tyrosine kinase, in prokaryotes as well as in eukaryotes, whose functioning is cyclic nucleotide-dependent.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1997.tb10448.x