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Autophosphorylation of nucleoside diphosphate kinase on non‐histidine residues
Author(s) -
Bominaar Anthony A.,
Tepper Annemiek D.,
Véron Michel
Publication year - 1994
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(94)00997-x
Subject(s) - autophosphorylation , histidine kinase , histidine , phosphorylation , biochemistry , kinase , nucleoside diphosphate kinase , allosteric regulation , enzyme , chemistry , active site , histidine decarboxylase , biology , protein kinase a
Recently, several reports appeared which described auto‐phosphorylation of NDP kinase on residues different from the active‐site histidine. Based on these findings conclusions were drawn with respect to a regulation of enzyme activity and to a possible role as a metastasis suppressor. In this paper we show that although non‐histidine autophosphorylation occurs on NDP kinases from mammals, lower eukaryotes and bacteria, less than 0.2% of the subunits are phosphorylated. Using site‐directed mutagenesis, we show that the active site histidine is essential for non‐histidine autophosphorylation. The low stoichiometry of phosphate incorporation excludes a role of autophosphorylation in regulating overall enzyme activity.