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Inhibition of nucleoside diphosphate kinase (NDPK/nm23) by cAMP analogues
Author(s) -
Anciaux Katelijne,
Van Dommelen Kristof,
Willems Roel,
Roymans Dirk,
Slegers Herman
Publication year - 1997
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/s0014-5793(96)01358-0
Subject(s) - nucleoside diphosphate kinase , phosphotransferase , autophosphorylation , biochemistry , chemistry , intracellular , enzyme , serine , phosphorylation , kinase , nucleoside , protein kinase a
Nucleoside diphosphate kinase (NDPK/nm23) ATP/GDP phosphotransferase activity and serine autophosphorylation is inhibited by N 6 ‐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. N 6 ‐mbcAMP is a substrate of the enzyme. DbcAMP and O ′ 2 ‐mbcAMP, cAMP analogues with a modified O ′ 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.