FEBS Letters | |
Autophosphorylation of nucleoside diphosphate kinase on non‐histidine residues | |
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
【 预 览 】
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