抄録
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 τ isoform exhibited intrinsic nucleoside diphosphate (NDP) kinase-like activity. 14-3-3 proteins preferentially catalyzed the transfer of the γ-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.
本文言語 | 英語 |
---|---|
ページ(範囲) | 244-248 |
ページ数 | 5 |
ジャーナル | FEBS Letters |
巻 | 419 |
号 | 2-3 |
DOI | |
出版ステータス | 出版済み - 15-12-1997 |
All Science Journal Classification (ASJC) codes
- 生物理学
- 構造生物学
- 生化学
- 分子生物学
- 遺伝学
- 細胞生物学