Inhibition of nucleoside diphosphate kinase (NDPK/nm23) by cAMP analogues

FEBS Letters
K AnciauxH Slegers

Abstract

Nucleoside diphosphate kinase (NDPK/nm23) ATP/GDP phosphotransferase activity and serine autophosphorylation is inhibited by N6-mbcAMP, 8-ClcAMP and 8-BrcAMP. Inhibition of the enzymatic activity largely depends on the concentration of ATP and becomes significant at ATP concentrations up to 0.5 mM and at effector concentrations measured in C6 cells stimulated with 1 mM cAMP analogue. N6-mbcAMP is a substrate of the enzyme. DbcAMP and 0'2-mbcAMP, cAMP analogues with a modified 0'2-ribose, did not affect the NDPK activity. Cyclic AMP is only a moderate inhibitor of NDPK even at low ATP concentrations. Possible inhibitory effects of cAMP and cAMP analogues on reported extra- and intracellular functions of NDPK/nm23 are discussed.

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Citations

Apr 29, 2009·Molecular and Cellular Biochemistry·Kate J TreharneAnil Mehta
Mar 26, 2011·Purinergic Signalling·Lucia Semianrio-VidalEduardo Rodolfo Lazarowski
Jun 7, 2017·Journal of Experimental Botany·Marcin LuzarowskiAleksandra Skirycz
Jun 5, 1998·The Journal of Biological Chemistry·R WillemsH Slegers
Oct 24, 1998·The Journal of Biological Chemistry·B SchneiderD Deville-Bonne
Sep 15, 2001·American Journal of Physiology. Heart and Circulatory Physiology·I L BuxtonD J Cheek
Jan 15, 2014·Acta Crystallographica. Section F, Structural Biology Communications·Florian GeorgescauldAlain Dautant
Jan 10, 2021·Life Sciences·Liting YuChangying Guo

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