Binding of ATP to nucleoside-diphosphate kinase: a kinetic study.
The binding of nucleotides to pig heart nucleoside-diphosphate kinase was studied using Rose Bengal as an optical probe. ATP, in the absence of Mg2+, binds slowly to the enzyme, with a second order rate constant of about 3000 M-1 . s-1, whereas in its presence the binding is much faster. This finding suggests the regulation of the nucleoside-diphosphate kinase activity by uncomplexed ATP, and that ATP binds normally to the enzyme via a metal ion bridge.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology; D009701:Nucleoside-Diphosphate Kinase / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D011487:Protein Conformation; D012395:Rose Bengal; D013552:Swine
D012395:Rose Bengal; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D009701:Nucleoside-Diphosphate Kinase; D008274:Magnesium