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Binding of ATP to nucleoside‐diphosphate kinase: a kinetic study
Author(s) -
Lascu Ioan,
Presecan Elena,
Proinov Ioan
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80715-3
Subject(s) - nucleoside diphosphate kinase , chemistry , nucleoside , adenosine triphosphate , biochemistry , adenosine diphosphate , kinase , medicine , platelet , platelet aggregation
The binding of nucleotides to pig heart nucleoside‐diphosphate kinase was studied using Rose Bengal as an optical probe. ATP, in the absence of Mg 2+ , 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.