Autophosphorylation of nucleoside diphosphate kinase on non‐histidine residues

FEBS Letters

Bominaar, Anthony A.¹  Véron, Michel¹  Tepper, Annemiek D.¹ 

[1] Unité de Biochimie Cellulaire, CNRS-URA 1129, Institut Pasteur, 75724 Paris Cedex 15, France

关键词: NDP kinase;    nm23;    Phosphorylation;    NDP;    nucleoside diphosphate;    SDS-PAGE;    SDS-polyacrylamine gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)00997-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown