Hydrogen phosphonatoacetate(2-)

• 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
• 英文名称: Hydrogen phosphonatoacetate(2-)
• 英文别名: 2-[hydroxy(oxido)phosphoryl]acetate
• 化学式: C₂H₂O₅P*H
• 分子量: 138.017
• InChiKey: XUYJLQHKOGNDPB-UHFFFAOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -2.2
• 重原子数：
  8
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  101
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  钷 、 Hydrogen phosphonatoacetate(2-) 生成
  参考文献：
  名称：

  Elesin, A. A.; Zaitsev, A. A.; Kazakova, S. S., Radiokhimiya, 1972, vol. 14, p. 558 - 562

  摘要：

  DOI：
• 作为产物：
  描述：

  水 、 nicotinamide adenine dinucleotide 、 phosphonoacetaldehyde 生成 氢(+1)阳离子 、 NADH 、 Hydrogen phosphonatoacetate(2-)
  参考文献：
  名称：

  膦酰乙醛脱氢酶的结构和功能：膦酰乙酸形成中的缺失环节

  摘要：

  膦酸盐 (C-PO32-) 可用作抗生素、除草剂和洗涤剂。在某些环境中，这些分子代表了磷的主要来源，并且一些微生物已经进化出专门用于膦酸盐降解的酶促机制。例如，最常见的天然存在的膦酸酯可以分解代谢为膦酰乙醛或膦酰乙酸酯，然后可以水解分别生成无机磷酸盐和乙醛或乙酸盐。膦酰乙醛氧化酶基因 (phnY) 将这两个水解过程联系起来，并为微生物代谢组中的膦酰乙酸酯产生提供了一种以前未知的分解代谢机制。在这里，我们展示了 PhnY 的生化表征和 apo 状态的高分辨率晶体结构，以及与底物、辅因子、和产品。活性位点突变体的动力学分析证明了高度保守的醛脱氢酶活性位点如何在自然界中被修饰以产生与膦酸酯底物的活性。

  DOI：

  10.1016/j.chembiol.2013.11.006

文献信息

• In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F
  作者：G McMullan、J P Quinn

  DOI：10.1128/jb.176.2.320-324.1994

  日期：1994.1

  A novel, metal-dependent, carbon-phosphorus bond cleavage activity, provisionally named phosphonoacetate hydrolase, was detected in crude extracts of Pseudomonas fluorescens 23F, an environmental isolate able to utilize phosphonoacetate as the sole carbon and phosphorus source. The activity showed unique specificity toward this substrate; its organic product, acetate, was apparently metabolized by

  在荧光假单胞菌23F的粗提物中检测到了一种新的，依赖金属的碳-磷键裂解活性（临时命名为膦酰基乙酸酯水解酶），后者是一种环境分离物，能够利用磷酰乙酸酯作为唯一的碳和磷源。活性对这种底物表现出独特的特异性。它的有机产物乙酸盐显然被宿主细胞的乙醛酸循环酶代谢。与在荧光假单胞菌23F的粗提物中也检测到的磷酸酶不同，膦酰乙酸水解酶仅在其唯一底物存在时才可诱导，并且不需要磷酸饥饿。
• The Purification and Properties of Phosphonoacetate Hydrolase, a Novel Carbon-Phosphorus Bond-Cleavage Enzyme from Pseudomonas Fluorescens 23F
  作者：John W. McGrath、G. Brian Wisdom、Geoffrey McMullan、Michael J. Larkin、John P. Quinn

  DOI：10.1111/j.1432-1033.1995.225_c.x

  日期：1995.11

  A novel, inducible, carbon-phosphorus bond-cleavage enzyme, phosphonoacetate hydrolase, was purified from cells of Pseudomonas fluorescens 23F grown on phosphonoacetate. The native enzyme had a molecular mass of approximately 80 kDa and, upon SDS/PAGE, yielded a homogenous protein band with an apparent molecular mass of about 38 kDa. Activity of purified phosphonoacetate hydrolase was Zn2+ dependent

  从生长在膦酰乙酸上的荧光假单胞菌23F的细胞中纯化出一种新颖的，可诱导的碳-磷键裂解酶，膦酰乙酸酯水解酶。天然酶具有约80kDa的分子量，并且在SDS / PAGE时，产生具有约38kDa的表观分子量的均质蛋白条带。纯化的膦酰基乙酸酯水解酶的活性依赖于Zn2 +，并且显示的最佳pH和最佳温度分别约为7.8和37摄氏度。纯化的酶的唯一底物膦酰基乙酸盐的表观Km为1.25 mM，并被结构类似物3-膦酰基丙酸酯和膦酸甲酸酯抑制。前19个氨基酸的NH2末端序列与其他数据库序列无显着相似性。
• Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon–phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida
  作者：Anna N Kulakova、Leonid A Kulakov、John P. Quinn

  DOI：10.1016/s0378-1119(97)00151-0

  日期：1997.8

  gene encoding a novel carbon-phosphorus bond cleavage enzyme, phosphonoacetate hydrolase, from Pseudomonas fluorescens 23F was cloned and expressed in Escherichia coli and Pseudomonas putida. It conferred on the latter host the ability to mineralize phosphonoacetate but on the former the ability to utilize it as sole phosphorus source only. The nucleotide and deduced amino acid sequences of the phnA

  克隆了编码荧光假单胞菌23F的新型碳-磷键裂解酶膦酰乙酸水解酶的phnA基因，并在大肠杆菌和恶臭假单胞菌中表达。它赋予后者宿主矿化膦酰乙酸的能力，而赋予后者宿主仅将其用作唯一磷源的能力。phnA基因的核苷酸和推导的氨基酸序列与任何数据库入选均未显示出显着同源性。
• A metal-independent hydrolase from a<i>Penicillium oxalicum</i>strain able to use phosphonoacetic acid as the only phosphorus source
  作者：Magdalena Klimek-Ochab、Barbara Lejczak、Giuseppe Forlani

  DOI：10.1016/s0378-1097(03)00301-x

  日期：2003.5

  A Penicillium oxalicum strain was capable of the phosphate-sensitive utilization of phosphonoacetic acid as the sole source of phosphorus. A carbon-to-phosphorus bond-cleavage enzyme yielding acetic acid and inorganic phosphate was detected and characterized in extracts from cells grown on this phosphonate. Contrary to bacterial phosphonoacetate hydrolases, the fungal enzyme neither required nor was stimulated by divalent cations. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
• Phosphonoacetate hydrolase from Penicillium oxalicum: Purification and properties, phosphate starvation-independent expression, and partial sequencing
  作者：Magdalena Klimek-Ochab、Giuseppe Raucci、Barbara Lejczak、Giuseppe Forlani

  DOI：10.1016/j.resmic.2005.06.002

  日期：2006.3

  The enzyme responsible for the hydrolysis of phosphonoacetic acid, a non-biogenic C-P compound, was purified to electrophoretic homogeneity from a wild-type strain of Penicillium oxalicum. A 50-fold enrichment was obtained by a combination of anion exchange, hydrophobic interaction and MonoQ-fast protein liquid chromatography, with a yield of one-third of the initial activity. A characterization of the protein showed both similarities and differences with respect to the well-characterized bacterial counterpart. The fungal phosphonoacetate hydrolase is a 43-kDa monomeric protein showing low affinity toward its substrate and high sensitivity to even mildly acidic pH values. Enzyme activity neither required nor was stimulated by the presence of divalent cations. Polyclonal antibodies were raised in mouse against the purified protein, allowing the study of enzyme induction as a function of the phosphate status of the cell. Peptide mass mapping led to the determination of about 20% of the primary structure. Despite the biochemical differences, amino acid alignment showed a high degree of similarity of the fungal hydrolase with the few sequences available to date for the bacterial enzyme. The possible physiological role of a phosphonoacetate hydrolase is discussed. (c) 2005 Elsevier SAS. All rights reserved.