Binding of ATP to nucleoside-diphosphate kinase: a kinetic study |
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Authors: | I Lascu E Presecan I Proinov |
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Affiliation: | Department of Biochemistry, Medical and Pharmaceutical Institute, Pasteur Street 6, R-3400 Cluj-Napoca, Romania |
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Abstract: | 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. |
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