Binding of ATP to nucleoside‐diphosphate kinase: a kinetic study

FEBS Letters

Presecan, Elena¹  Lascu, Ioan¹  Proinov, Ioan¹ 

[1] Department of Biochemistry, Medical and Pharmaceutical Institute, Pasteur Street 6, R-3400 Cluj-Napoca, Romania

关键词: Nucleoside-diphosphate kinase;    Rose Bengal;    Substrate binding;    Metal ion bridge;    Conformational change;    ATP-Mg2+ complex;   

DOI  :  10.1016/0014-5793(86)80715-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown