膦酰乙醛 | 16051-76-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机膦酸及其衍生物
• 中文名称: 膦酰乙醛
• 英文名称: phosphonoacetalhdehyde
• 英文别名: phosphonoacetaldehyde；formyl methyl phosphonic acid；Formylmethyl-phosphonsaeure；2-Oxo-aethylphosphonsaeure；2-Phosphonoacetaldehyd；2-oxoethylphosphonic acid
• CAS: 16051-76-6
• 化学式: C₂H₅O₄P
• 分子量: 124.033
• InChiKey: YEMKIGUKNDOZEG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  74.6
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 海关编码：
  2931900090

反应信息

• 作为反应物：
  描述：

  膦酰乙醛 在 Streptomyces hygroscopicus 26 作用下， 以 various solvent(s) 为溶剂， 反应 96.0h， 以0.2 mg的产率得到bialaphos
  参考文献：
  名称：

  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.

  摘要：

  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。

  DOI：

  10.7164/antibiotics.50.212
• 作为产物：
  描述：

  phosphoenolpyruvic acid monopotassium salt 在 Ppd-Bf-His enzyme 、 RhiH-N-His enzyme 、 焦磷酸硫胺素 、 magnesium chloride 作用下， 反应 0.75h， 生成 膦酰乙醛
  参考文献：
  名称：

  Biosynthesis of Rhizocticins, Antifungal Phosphonate Oligopeptides Produced by Bacillus subtilis ATCC6633

  摘要：

  Rhizocticins are phosphonate oligopeptide antibiotics containing the C-terminal nonproteinogenic amino acid (Z)-L-2-amino-5-phosphono-3-pentenoic acid (APPA). Here we report the identification and characterization of the rhizocticin biosynthetic gene cluster (rhi) in Bacillus subtilis ATCC6633. Rhizocticin B was heterologously produced in the nonproducer strain Bacillus subtilis 168. A biosynthetic pathway is proposed on the basis of bioinformatics analysis of the rhi genes. One of the steps during the biosynthesis of APPA is an unusual aldol reaction between phosphonoacetaldehyde and oxaloacetate catalyzed by an aldolase homolog RhiG. Recombinant RhiG was prepared, and the product of an in vitro enzymatic conversion was characterized. Access to this intermediate allows for biochemical characterization of subsequent steps in the pathway.

  DOI：

  10.1016/j.chembiol.2009.11.017

文献信息

• Reaction of HppE with Substrate Analogues: Evidence for Carbon–Phosphorus Bond Cleavage by a Carbocation Rearrangement
  作者：Wei-chen Chang、Steven O. Mansoorabadi、Hung-wen Liu

  DOI：10.1021/ja403441x

  日期：2013.6.5

  (S)-2-hydroxypropylphosphonic acid ((S)-2-HPP) epoxidase (HppE) is an unusual mononuclear non-heme iron enzyme that catalyzes the oxidative epoxidation of (S)-2-HPP in the biosynthesis of the antibiotic fosfomycin. Recently, HppE has been shown to accept (R)-1-hydroxypropylphosphonic acid as a substrate and convert it to an aldehyde product in a reaction involving a biologically unprecedented 1,2-phosphono

  (S)-2-羟丙基膦酸 ((S)-2-HPP) 环氧化酶 (HppE) 是一种不寻常的单核非血红素铁酶，可在抗生素磷霉素的生物合成中催化 (S)-2-HPP 的氧化环氧化. 最近，HppE 已被证明接受 (R)-1-羟丙基膦酸作为底物，并在涉及生物学上前所未有的 1,2-膦酰基迁移的反应中将其转化为醛产物。在这项研究中，设计、合成了一系列底物类似物，并将其用作机械探针来研究这种新型酶促转化。所得数据以及从密度泛函理论计算中获得的见解与 HppE 催化的膦酰基迁移的机制一致，该机制涉及碳正离子中间体的形成。像这样，
• Biosynthesis of the Fungal Organophosphonate Fosfonochlorin Involves an Iron(II) and 2‐(Oxo)glutarate Dependent Oxacyclase
  作者：Simanga R. Gama、Toda Stankovic、Kendall Hupp、Ahmed Al Hejami、Mimi McClean、Alysa Evans、Diane Beauchemin、Friedrich Hammerschmidt、Katharina Pallitsch、David L. Zechel

  DOI：10.1002/cbic.202100352

  日期：2022.1.19

  Early steps in the biosynthesis of the organophosphonate Fosfonochlorin are revealed, including a rare example of oxidative cyclization of an alcohol to form an epoxide.

  揭示了有机膦酸盐磷酰草胺生物合成的早期步骤，包括一个罕见的醇氧化环化形成环氧化物的例子。
• Fridland,S.V. et al., Journal of general chemistry of the USSR, 1969, vol. 39, p. 1949 - 1950
  作者：Fridland,S.V. et al.

  DOI：——

  日期：——
• Lee, Sheng-Lian; Hepburn, Timothy W.; Swartz, William H., Journal of the American Chemical Society, 1992, vol. 114, # 19, p. 7346 - 7354
  作者：Lee, Sheng-Lian、Hepburn, Timothy W.、Swartz, William H.、Ammon, Herman L.、Mariano, Patrick S.、Dunaway-Mariano, Debra

  DOI：——

  日期：——
• Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage
  作者：Sushmita D. Lahiri、Guofeng Zhang、Debra Dunaway-Mariano、Karen N. Allen

  DOI：10.1016/j.bioorg.2006.09.007

  日期：2006.12

  Phosphonatase functions in the 2-aminoethylphosphonate (AEP) degradation pathway of bacteria, catalyzing the hydrolysis of the C-P bond in phosphonoacetaldehyde (Pald) via formation of a bi-covalent Lys53ethylenamine/Asp12 aspartylphosphate intermediate. Because phosphonatase is a member of the haloacid dehalogenase superfamily, a family predominantly comprised of phosphatases, the question arises as to how this new catalytic activity evolved. The source of general acid-base catalysis for Schiff-base formation and aspartylphosphate hydrolysis was probed using pH-rate profile analysis of active-site mutants and X-ray crystallographic analysis of modified forms of the enzyme. The 2.9 A X-ray crystal structure of the mutant Lys53Arg complexed with Mg2+ and phosphate shows that the equilibrium between the open and the closed conformation is disrupted, favoring the open conformation. Thus, proton dissociation from the cap domain Lys53 is required for cap domain-core domain closure. The likely recipient of the Lys53 proton is a water-His56 pair that serves to relay the proton to the carbonyl oxygen of the phosphonoacetaldehyde (Pald) substrate upon addition of the Lys53. The pH-rate profile analysis of active-site mutants was carried out to test this proposal. The proximal core domain residues Cys22 and Tyr128 were ruled out, and the role of cap domain His56 was supported by the results. The X-ray crystallographic structure of wild-type phosphonatase reduced with NaBH4 in the presence of Pald was determined at 2.4A resolution to reveal N epsilon-ethyl-Lys53 juxtaposed with a sulfate ligand bound in the phosphate site. The position of the C2 of the N-ethyl group in this structure is consistent with the hypothesis that the cap domain N epsilon-ethylenamine-Lys53 functions as a general base in the hydrolysis of the aspartylphosphate bi-covalent enzyme intermediate. Because the enzyme residues proposed to play a key role in P-C bond cleavage are localized on the cap domain, this domain appears to have evolved to support the diversification of the HAD phosphatase core domain for catalysis of hydrolytic P-C bond cleavage.