methoxymalonic acid | 57584-77-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: methoxymalonic acid
• 英文别名: Methoxy-malonsaeure；O-Methyl-tartronsaeure；2-methoxypropanedioic acid
• CAS: 57584-77-7
• 化学式: C₄H₆O₅
• mdl: MFCD19229038
• 分子量: 134.089
• InChiKey: VLDSMCHWNWDAKQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.5
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  83.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methoxymalonic acid 在 N,N-二甲基甲酰胺 草酰氯 作用下， 以 二氯甲烷 为溶剂， 生成 methoxymalonyl dichloride
  参考文献：
  名称：

  ATPENINS

  摘要：

  本发明涉及制备特定2-吡啶酮和2-吡啶醇的过程，涉及这两种类型的新化合物以及它们作为生物活性化合物的用途，特别是用于控制农作物保护中的有害微生物，在医药领域和材料保护中。

  公开号：

  US20100168175A1
• 作为产物：
  描述：

  甲氧基马来酸二甲酯 在 水 、 sodium hydroxide 作用下， 以100%的产率得到methoxymalonic acid
  参考文献：
  名称：

  Enzymatic Extender Unit Generation for In Vitro Polyketide Synthase Reactions: Structural and Func-tional Showcasing of Streptomyces coelicolor MatB

  摘要：

  In vitro experiments with modular polyketide synthases (PKSs) are often limited by the availability of polyketide extender units. To determine the polyketide extender units that can be biocatalytically accessed via promiscuous malonyl-CoA ligases, structural and functional studies were conducted on Streptomyces coelicolor MatB. We demonstrate that this adenylate-forming enzyme is capable of producing most CoA-linked polyketide extender units as well as pantetheine- and N-acetylcysteamine-linked analogs useful for in vitro PKS studies. Two ternary product complex structures, one containing malonyl-CoA and AMP and the other containing (2R)-methylmalonyl-CoA and AMP, were solved to 1.45 angstrom and 1.43 angstrom resolution, respectively. MatB crystallized in the thioester-forming conformation, making extensive interactions with the bound extender unit products. This first structural characterization of an adenylate-forming enzyme that activates diacids reveals the molecular details for how malonate and its derivatives are accepted. The orientation of the alpha-methyl group of bound (2R)-methylmalonyl-CoA, indicates that it is necessary to epimerize alpha-substituted extender units formed by MatB before they can be accepted by PKS acyltransferase domains. We demonstrate the in vitro incorporation of methylmalonyl groups ligated by MatB to CoA, pantetheine, or N-acetylcysteamine into a triketide pyrone by the terminal module of the 6-deoxyerythronolide B synthase. Additionally, a means for quantitatively monitoring certain in vitro PKS reactions using MatB is presented.

  DOI：

  10.1016/j.chembiol.2010.12.014

文献信息

• Poly Specific <i>trans</i>-Acyltransferase Machinery Revealed <i>via</i> Engineered Acyl-CoA Synthetases
  作者：Irina Koryakina、John McArthur、Shan Randall、Matthew M. Draelos、Ewa M. Musiol、David C. Muddiman、Tilmann Weber、Gavin J. Williams

  DOI：10.1021/cb3003489

  日期：2013.1.18

  Polyketide synthases construct polyketides with diverse structures and biological activities via the condensation of extender units and acyl thioesters. Although a growing body of evidence suggests that polyketide synthases might be tolerant to non-natural extender units, in vitro and in vivo studies aimed at probing and utilizing polyketide synthase specificity are severely limited to only a small

  聚酮化合物合酶通过增量剂单元和酰基硫酯的缩合来构建具有多种结构和生物活性的聚酮化合物。尽管越来越多的证据表明，聚酮化合物合酶可能在体外和体内都可以耐受非天然扩展剂由于缺乏合成多种酰基辅酶A增量剂单元的途径，旨在探索和利用聚酮化合物合酶特异性的研究被严格限制在仅少量的增量剂单元中。在这里，我们报告了混杂的丙二酰-CoA合成酶变体的构建，该变体可用于合成在C2位置取代的大范围的丙二酰-CoA扩展剂单元，其中一些包含用于化学选择性连接的手柄，在天然生物合成中未发现系统。我们通过探究几种反式的酰基辅酶A特异性突出了这些酶的效用。-酰基转移酶，导致对非天然延伸单元的多特异性的空前发现，其中几种在天然生物合成途径中未发现。这些结果表明，聚酮化合物的生物合成机制对非天然底物的耐受性可能比以前建立的更高，并且突变体合成酶是探测生物合成机制特异性的有价值的工具。我们的数据提出了利用这种滥交和实现聚酮化合物的区域选择性修饰的新的合成生物学策略。
• Kadesch, Journal of the American Chemical Society, 1946, vol. 68, p. 44
  作者：Kadesch

  DOI：——

  日期：——
• Swan, George A., Journal of the Chemical Society. Perkin transactions I, 1985, p. 1757 - 1766
  作者：Swan, George A.

  DOI：——

  日期：——
• ATPENINS
  申请人：ADELT Isabelle

  公开号：US20100168175A1

  公开（公告）日：2010-07-01

  The present invention relates to processes for preparing certain 2-pyridones and 2-pyridinols, to novel compounds of these two types and to their use as biologically active compounds, in particular for controlling harmful microorganisms in crop protection, in the medicinal field and in the protection of materials.

  本发明涉及制备特定2-吡啶酮和2-吡啶醇的过程，涉及这两种类型的新化合物以及它们作为生物活性化合物的用途，特别是用于控制农作物保护中的有害微生物，在医药领域和材料保护中。
• Enzymatic Extender Unit Generation for In Vitro Polyketide Synthase Reactions: Structural and Func-tional Showcasing of Streptomyces coelicolor MatB
  作者：Amanda J. Hughes、Adrian Keatinge-Clay

  DOI：10.1016/j.chembiol.2010.12.014

  日期：2011.2

  In vitro experiments with modular polyketide synthases (PKSs) are often limited by the availability of polyketide extender units. To determine the polyketide extender units that can be biocatalytically accessed via promiscuous malonyl-CoA ligases, structural and functional studies were conducted on Streptomyces coelicolor MatB. We demonstrate that this adenylate-forming enzyme is capable of producing most CoA-linked polyketide extender units as well as pantetheine- and N-acetylcysteamine-linked analogs useful for in vitro PKS studies. Two ternary product complex structures, one containing malonyl-CoA and AMP and the other containing (2R)-methylmalonyl-CoA and AMP, were solved to 1.45 angstrom and 1.43 angstrom resolution, respectively. MatB crystallized in the thioester-forming conformation, making extensive interactions with the bound extender unit products. This first structural characterization of an adenylate-forming enzyme that activates diacids reveals the molecular details for how malonate and its derivatives are accepted. The orientation of the alpha-methyl group of bound (2R)-methylmalonyl-CoA, indicates that it is necessary to epimerize alpha-substituted extender units formed by MatB before they can be accepted by PKS acyltransferase domains. We demonstrate the in vitro incorporation of methylmalonyl groups ligated by MatB to CoA, pantetheine, or N-acetylcysteamine into a triketide pyrone by the terminal module of the 6-deoxyerythronolide B synthase. Additionally, a means for quantitatively monitoring certain in vitro PKS reactions using MatB is presented.