Yano M, Mori S, Niwa Y, Inoue M, Kido H
Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Japan.
FEBS Lett. 1997 Dec 15;419(2-3):244-8. doi: 10.1016/s0014-5793(97)01469-5.
14-3-3 proteins play a role in many cellular functions as molecular chaperone and adapter proteins: they bind to and modulate several proteins involved in cell proliferation and differentiation, and also function ATP-dependently in targeting of precursors to mitochondria. We show here that 14-3-3 purified from a human lymphoblastoma and also its recombinant tau isoform exhibited intrinsic nucleoside diphosphate (NDP) kinase-like activity. 14-3-3 proteins preferentially catalyzed the transfer of the gamma-phosphate group from ATP, dATP or dGTP to all nucleoside diphosphates and this transfer involved acid-labile phosphoenzyme intermediates. They also simultaneously catalyzed the reverse reaction of ATP hydrolysis. These properties of 14-3-3 are similar to those of NDP kinase, but not to those of adenylate kinase.
14-3-3蛋白作为分子伴侣和衔接蛋白在许多细胞功能中发挥作用：它们与多种参与细胞增殖和分化的蛋白质结合并对其进行调节，并且还以ATP依赖的方式在将前体靶向线粒体的过程中发挥作用。我们在此表明，从人淋巴瘤中纯化的14-3-3蛋白及其重组tau亚型表现出内在的核苷二磷酸（NDP）激酶样活性。14-3-3蛋白优先催化γ-磷酸基团从ATP、dATP或dGTP转移至所有核苷二磷酸，并且这种转移涉及酸不稳定的磷酸酶中间体。它们还同时催化ATP水解的逆反应。14-3-3蛋白的这些特性与NDP激酶的特性相似，但与腺苷酸激酶的特性不同。
