title: Direct activation of guanine nucleotide binding proteins through a high-energy phosphate-transfer by nucleoside diphosphate-kinase.
abstract: An in vitro study of phosphate-transfer, from the high-energy phosphates on the phosphoenzyme (enzyme-bound high-energy phosphate intermediate) of NDP-kinase to GDP on various guanine nucleotide binding proteins (G1, elongation factor alpha 1, recombinant v-rasH p21 protein, transducin, Gi and Go), revealed that the GDP acts as a phosphate-acceptor, in the presence of divalent cations (Mg2+ and Ca2+). This finding suggests that via phosphate-transfer, NDP-kinase may be responsible for the direct activation of various guanine nucleotide binding proteins through phosphate-transfer by the enzyme.
authors.affiliation: Department of Bacteriology, Tohoku University School of Medicine, Sendai, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ohtsuki
authors.forename: M
authors.initials: M
authors.lastname: Yokoyama
mesh_terms: D019204:GTP-Binding Proteins / Q000378:metabolism*; D006150:Guanine Nucleotides / Q000378:metabolism*; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006153:Guanosine Diphosphate / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D009701:Nucleoside-Diphosphate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013873:Thionucleotides / Q000378:metabolism
chemical_list: D006150:Guanine Nucleotides; D013873:Thionucleotides; D006153:Guanosine Diphosphate; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006160:Guanosine Triphosphate; D010770:Phosphotransferases; D009701:Nucleoside-Diphosphate Kinase; D019204:GTP-Binding Proteins