Laussmann T, Reddy K M, Reddy K K, Falck J R, Vogel G
Fachbereich 9 - Chemie, Bergische Universität GHS Wuppertal, Federal Republic of Germany.
Biochem J. 1997 Feb 15;322 ( Pt 1)(Pt 1):31-3. doi: 10.1042/bj3220031.
Two diphospho-myo-inositol phosphates from Dictyostelium were recently investigated by two-dimensional 1H/31P NMR analysis and assigned to be either D-4-diphospho-myo-inositol pentakisphosphate (D-4-PP-InsP5) and D-4,5-bisdiphospho-myo-inositol tetrakisphosphate (D-4,5-bis-PP-InsP4) or their corresponding enantiomers D-6-PP-InsP5 and D-5,6-bis-PP-InsP4. In the present study the naturally occurring enantiomers were identified by using defined synthetic PP-InsP5 isomers as substrates for a partially purified PP-InsP5 5-kinase from Dictyostelium. This enzyme specifically phosphorylates the naturally occurring PP-InsP5 and the synthetic D-6-PP-InsP5, leading to D-5,6-bis-PP-InsP4. In contrast, neither D-4-PP-InsP5 nor D-1-PP-InsP5 or D-3-PP-InsP5 are converted by the enzyme.
最近通过二维1H/31P NMR分析对来自盘基网柄菌的两种二磷酸肌醇磷酸进行了研究,并确定它们为D-4-二磷酸肌醇五磷酸(D-4-PP-InsP5)和D-4,5-双二磷酸肌醇四磷酸(D-4,5-双-PP-InsP4)或它们相应的对映体D-6-PP-InsP5和D-5,6-双-PP-InsP4。在本研究中,通过使用确定的合成PP-InsP5异构体作为来自盘基网柄菌的部分纯化的PP-InsP5 5-激酶的底物,鉴定了天然存在的对映体。该酶特异性地磷酸化天然存在的PP-InsP5和合成的D-6-PP-InsP5,生成D-5,6-双-PP-InsP4。相反,该酶不会将D-4-PP-InsP5、D-1-PP-InsP5或D-3-PP-InsP5转化。