3-膦酰丙酮酸 | 5824-58-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 中文名称: 3-膦酰丙酮酸
• 英文名称: 3‐phosphopyruvate
• 英文别名: phosphonopyruvic acid；phosphonopyruvate；2-oxo-3-phosphonopropanoic acid
• CAS: 5824-58-8
• 化学式: C₃H₅O₆P
• 分子量: 168.043
• InChiKey: CHDDAVCOAOFSLD-UHFFFAOYSA-N

物化性质

• 溶解度：
  甲醇（微溶）、水（微溶）

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  10
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  112
• 氢给体数：
  3
• 氢受体数：
  6

安全信息

• 海关编码：
  2931900090

反应信息

• 作为反应物：
  描述：

  3-膦酰丙酮酸 在 PEP phosphomutase 作用下， 以 水 为溶剂， 生成 磷烯醇丙酮酸
  参考文献：
  名称：

  Evidence for an intramolecular, stepwise reaction pathway for PEP phosphomutase catalyzed phosphorus-carbon bond formation

  摘要：

  The Tetrahymena pyriformis enzyme, phosphoenolpyruvate phosphomutase, catalyzes the rearrangement of phosphoenolpyruvate to the P-C bond containing metabolite, phosphonopyruvate. To distinguish between an intra- and intermolecular reaction pathway for this process an equimolar mixture of [P-O-18,C(2)-O-18]thiophosphonopyruvate and (all O-16) thiophosphonopyruvate was reacted with the phosphomutase, and the resulting products were analyzed by P-31 NMR. The absence of the cross-over product [C(2)-O-18]thiophosphonoenolpyruvate in the product mixture was interpreted as evidence for an intramolecular reaction pathway. To distinguish between a concerted and stepwise intramolecular reaction pathway the pure enantiomers of the chiral substrate [O-18]thiophosphonopyruvate were prepared and the stereochemical course of their conversion to chiral [O-18]thiophosphoenolpyruvate was determined. The assignments of the phosphorus configurations in the [O-18]thiophosphonopyruvate enantiomers reported earlier (McQueney, M. S.; Lee, S.-l.; Bowman, E.; Mariano, P. S.; Dunaway-Mariano, D. J. Am. Chem. Soc. 1989, 111, 6885-6887) were revised according to the finding that introduction of the O-18 label into the thiophosphonopyruvate precursor occurs with retention rather than with (the previously assumed) inversion of configuration. On the basis the observed conversion of (S(p))-[O-18]thiophosphonopyruvate to (S(p))-[O-18]thiophosphoenolpyruvate and (R(p))-[O-18]thiophosphonopyruvate to (Rp)-[O-18]thiophosphoenolpyruvate, it was concluded that the PEP phosphomutase reaction proceeds with retention of the phosphorus configuration and therefore by a stepwise mechanism. Lastly, the similar reactivity of the oxo- and thio-substituted phosphonopyruvate substrates (i.e., nearly equal V(max)) was interpreted to suggest that nucleophilic addition to the phosphorus atom is not rate limiting among the reaction steps.

  DOI：

  10.1021/jo00025a031
• 作为产物：
  描述：

  Carboxyphosphonoenolpyruvate 生成 3-膦酰丙酮酸
  参考文献：
  名称：

  HIDAKA, TOMOMI;SETO, HARUO;IMAI, SATOSHI, J. AMER. CHEM. SOC., 111,(1989) N0, C. 8012-8013

  摘要：

  DOI：
• 作为试剂：
  描述：

  L-天门冬氨酸 在 3-膦酰丙酮酸 、 recombinant dipeptide ligase PnfD from Escherichia coli 作用下， 生成 L-(+)-2-氨基-3-膦酰基丙酸
  参考文献：
  名称：

  Biosynthesis of Bacillus Phosphonoalamides Reveals Highly Specific Amino Acid Ligation

  摘要：

  DOI：

  10.1021/acschembio.4c00190

文献信息

• Studies on the Biosynthesis of Bialaphos. Biochemical Mechanism of C-P Bond Formation: Discovery of Phosphonopyruvate Decarboxylase which Catalyzes the Formation of Phosphonoacetaldehyde from Phosphonopyruvate.
  作者：HIDEO NAKASHITA、KEI WATANABE、OSAMU HARA、TOMOMI HIDAKA、HARUO SETO

  DOI：10.7164/antibiotics.50.212

  日期：——

  The biosynthetic step following the phosphoenolpyruvate (PEP) phosphomutase reaction which forms a C-P bond of bialaphos was proven by the identification of phosphonopyruvate (PnPy) and phosphonoacetaldehyde (PnAA) as intermediates in the culture broth of Streptomyces hygroscopicus, a producing organism of bialaphos, and by detection of enzymatic decarboxylation of PnPy to PnAA. Purified PnPy decarboxylase turned out to require thiamine diphosphate and Mg2+ as cofactors. PnPy decarboxylase drives the unfavorable forward reaction to form PnPy catalyzed by PEP phosphomutase and is suggested to be essential to C-P compound biosynthesis.

  磷酸烯醇丙酮酸（PEP）磷酸化突变酶反应形成比亚拉磷（bialaphos）的 C-P 键之后的生物合成步骤，是通过在比亚拉磷（bialaphos）的生产生物--透明链霉菌（Streptomyces hygroscopicus）的培养液中鉴定出作为中间产物的磷酸烯醇丙酮酸（PnPy）和磷酰乙醛（PnAA），以及通过检测 PnPy 到 PnAA 的酶脱羧反应而得到证实的。纯化的 PnPy 脱羧酶需要二磷酸硫胺和 Mg2+ 作为辅助因子。PnPy 脱羧酶在 PEP 磷酸化酶的催化下驱动不利的正向反应生成 PnPy，并被认为是 C-P 化合物生物合成所必需的。
• Complete Biosynthetic Pathway of the Phosphonate Phosphonothrixin: Two Distinct Thiamine Diphosphate-Dependent Enzymes Divide the Work to Form a C–C Bond
  作者：Yuxun Zhu、Taro Shiraishi、Jianwen Lin、Keito Inaba、Atsuro Ito、Yusuke Ogura、Makoto Nishiyama、Tomohisa Kuzuyama

  DOI：10.1021/jacs.2c06546

  日期：2022.9.21

  catalyzes the transfer of a two-carbon unit attached to the thiamine diphosphate (TPP) cofactor (provided by the acetohydroxyacid synthase homologue, PtxB7) to HOPA to produce PTX. This study reveals a unique C–C bond formation in which two distinct TPP-dependent enzymes, PtxB5/6 and PtxB7, divide the work to transfer an acetyl group, highlighting an unprecedented biosynthetic strategy for natural products

  膦酸盐通常通过模仿生物分子的磷酸盐和羧酸盐来表现出生物活性。由土壤栖息细菌糖丝菌产生的膦酸盐磷酸丝菌素 (PTX)sp。ST-888，具有除草活性。在这项研究中，我们通过在体外重建其生物合成，提出了 PTX 的完整生物合成途径。我们的深入分析表明，两种脱氢酶一起将膦酰基丙酮酸 (PnPy) 还原为 2-羟基-3-膦酰基丙酸 (HPPA)，以加速磷酸烯醇丙酮酸 (PEP) 向 PnPy 的热力学不利重排。接下来的四种酶将 HPPA 转化为 (3-羟基-2-氧代丙基) 膦酸 (HOPA)。在 PTX 生物合成的最后阶段，“分裂基因”转酮醇酶同源物 PtxB5/6 催化连接到硫胺素二磷酸 (TPP) 辅因子（由乙酰羟酸合酶同源物 PtxB7 提供）上的两个碳单元转移到HOPA 生产 PTX。这项研究揭示了一种独特的 C-C 键形成，其中两种不同的 TPP 依赖性酶，
• Freeman, Sally; Irwin, William J.; Schwalbe, Carl H., Journal of the Chemical Society. Perkin transactions II, 1991, # 2, p. 263 - 267
  作者：Freeman, Sally、Irwin, William J.、Schwalbe, Carl H.

  DOI：——

  日期：——
• SPARKES, MICHAEL J.;ROGERS, KAREN L.;DIXON, HENRY B. E., EUR. J. BIOCHEM., 194,(1990) N, C. 373-376
  作者：SPARKES, MICHAEL J.、ROGERS, KAREN L.、DIXON, HENRY B. E.

  DOI：——

  日期：——
• Evidence for an intramolecular, stepwise reaction pathway for PEP phosphomutase catalyzed phosphorus-carbon bond formation
  作者：Michael S. McQueney、Sheng Lian Lee、William H. Swartz、Herman L. Ammon、Patrick S. Mariano、Debra Dunaway-Mariano

  DOI：10.1021/jo00025a031

  日期：1991.12

  The Tetrahymena pyriformis enzyme, phosphoenolpyruvate phosphomutase, catalyzes the rearrangement of phosphoenolpyruvate to the P-C bond containing metabolite, phosphonopyruvate. To distinguish between an intra- and intermolecular reaction pathway for this process an equimolar mixture of [P-O-18,C(2)-O-18]thiophosphonopyruvate and (all O-16) thiophosphonopyruvate was reacted with the phosphomutase, and the resulting products were analyzed by P-31 NMR. The absence of the cross-over product [C(2)-O-18]thiophosphonoenolpyruvate in the product mixture was interpreted as evidence for an intramolecular reaction pathway. To distinguish between a concerted and stepwise intramolecular reaction pathway the pure enantiomers of the chiral substrate [O-18]thiophosphonopyruvate were prepared and the stereochemical course of their conversion to chiral [O-18]thiophosphoenolpyruvate was determined. The assignments of the phosphorus configurations in the [O-18]thiophosphonopyruvate enantiomers reported earlier (McQueney, M. S.; Lee, S.-l.; Bowman, E.; Mariano, P. S.; Dunaway-Mariano, D. J. Am. Chem. Soc. 1989, 111, 6885-6887) were revised according to the finding that introduction of the O-18 label into the thiophosphonopyruvate precursor occurs with retention rather than with (the previously assumed) inversion of configuration. On the basis the observed conversion of (S(p))-[O-18]thiophosphonopyruvate to (S(p))-[O-18]thiophosphoenolpyruvate and (R(p))-[O-18]thiophosphonopyruvate to (Rp)-[O-18]thiophosphoenolpyruvate, it was concluded that the PEP phosphomutase reaction proceeds with retention of the phosphorus configuration and therefore by a stepwise mechanism. Lastly, the similar reactivity of the oxo- and thio-substituted phosphonopyruvate substrates (i.e., nearly equal V(max)) was interpreted to suggest that nucleophilic addition to the phosphorus atom is not rate limiting among the reaction steps.