Autophosphorylation of nucleoside diphosphate kinase on non-histidine residues.
Recently, several reports appeared which described auto-phosphorylation of NDP kinase on residues different from the active-site histidine. Based on these findings conclusions were drawn with respect to a regulation of enzyme activity and to a possible role as a metastasis suppressor. In this paper we show that although non-histidine autophosphorylation occurs on NDP kinases from mammals, lower eukaryotes and bacteria, less than 0.2% of the subunits are phosphorylated. Using site-directed mutagenesis, we show that the active site histidine is essential for non-histidine autophosphorylation. The low stoichiometry of phosphate incorporation excludes a role of autophosphorylation in regulating overall enzyme activity.
Bominaar
A A
AA
Unité de Biochimie Cellulaire, CNRS-URA 1129, Institut Pasteur, Paris, France.
Tepper
A D
AD
Véron
M
M
D000818:Animals; D001483:Base Sequence; D004023:Dictyostelium / Q000201:enzymology; D006639:Histidine / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D016941:Myxococcus xanthus / Q000201:enzymology; D009701:Nucleoside-Diphosphate Kinase / Q000378:metabolism*; D009838:Oligodeoxyribonucleotides; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding
D009838:Oligodeoxyribonucleotides; D010710:Phosphates; D006639:Histidine; D009701:Nucleoside-Diphosphate Kinase