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Direct activation of guanine nucleotide binding proteins through a high-energy phosphate-transfer by nucleoside diphosphate-kinase



Direct activation of guanine nucleotide binding proteins through a high-energy phosphate-transfer by nucleoside diphosphate-kinase



Biochemical and Biophysical Research Communications 148(1): 300-307



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.

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Accession: 039836243

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PMID: 2823806

DOI: 10.1016/0006-291x(87)91110-7


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