title: Autophosphorylation of nucleoside diphosphate kinase on non-histidine residues.
abstract: 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.
authors.affiliation: Unité de Biochimie Cellulaire, CNRS-URA 1129, Institut Pasteur, Paris, France.
authors.forename: A A
authors.initials: AA
authors.lastname: Bominaar
authors.forename: A D
authors.initials: AD
authors.lastname: Tepper
authors.forename: M
authors.initials: M
authors.lastname: Véron
mesh_terms: 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
chemical_list: D009838:Oligodeoxyribonucleotides; D010710:Phosphates; D006639:Histidine; D009701:Nucleoside-Diphosphate Kinase