3-maleylpyruvic acid | 89677-43-0

• 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
• 英文名称: 3-maleylpyruvic acid
• 英文别名: maleylacetone；4,6-dioxohept-2-enedioic acid
• CAS: 89677-43-0
• 化学式: C₇H₆O₆
• 分子量: 186.121
• InChiKey: AZCFLHZUFANAOR-UHFFFAOYSA-N

物化性质

• 沸点：
  421.8±30.0 °C(Predicted)
• 密度：
  1.535±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.7
• 重原子数：
  13
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.14
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  甲基氢醌 在 2,6-dichlorohydroquinone 1,2-dioxygenase 作用下， 生成 3-maleylpyruvic acid
  参考文献：
  名称：

  Substrate Specificity of Sphingobium chlorophenolicum 2,6-Dichlorohydroquinone 1,2-Dioxygenase

  摘要：

  PcpA is an aromatic ring-cleaving dioxygenase that is homologous to the well-characterized Fe(II)-dependent catechol, extradiol dioxygenases. This enzyme catalyzes the oxidative cleavage of 2,6-dichlorohydroquinone in the catabolism of pentachlorophenol by Sphingobium chlorophenolicum ATCC 39723. H-1 NMR and steady-state kinetics were used to determine the regiospecificity of ring cleavage and the substrate specificity of the enzyme. PcpA exhibits a high degree of substrate specificity for 2,6-disubstituted hydroquinones, with halogens greatly preferred at those positions. Notably, the k(cat)(app)/K-mA(app) of 2,6-dichlorohydroquinone is similar to 40-fold higher than that of 2,6-dimethylhydroquinone. The asymmetric substrate 2-chloro-6-methylhydroquinone yields a mixture of 1,2- and 1,6-cleavage products. These two modes of cleavage have different K-mO(app) values (21 and 260 mu M, respectively), consistent with a mechanism in which the substrate binds in two catalytically productive orientations. In contrast, monosubstituted hydroquinones show a limited amount of ring cleavage but rapidly inactivate the enzyme in an O-2-dependent fashion, suggesting that oxidation of the Fe(II) may be the cause. Potent inhibitors of PcpA include ortho-disubstituted phenols and 3-bromocatechol. 2,6-Dibromophenol is the strongest competitive inhibitor, consistent with PcpA's substrate specificity. Several factors that could yield this specificity for halogen substituents are discussed. Interestingly, 3-bromocatechol also inactivates the enzyme, while 2,6-dihalophenols do not, indicating a requirement for two hydroxyl groups for ring cleavage and for enzyme inactivation. These results provide mechanistic insights into the hydroquinone dioxygenases.

  DOI：

  10.1021/bi200855m

文献信息

• Metabolism of toxic benzonitrile and hydroxybenzonitrile isomers via several distinct central pathway intermediates in a catabolically robust Burkholderia sp.
  作者：Mriganka M. Karmakar、Satamita Deb、Tapan K. Dutta

  DOI：10.1016/j.bbrc.2024.149822

  日期：2024.5

  both humans and wildlife. In the present study, sp. strain BC1 was observed to be capable of utilizing toxic benzonitrile and hydroxybenzonitrile isomers singly, as sole carbon and energy sources. The results of chromatographic and spectrometric analyses in combination with oxygen uptake and enzyme activity studies, revealed the metabolism of benzonitrile as well as 2-, 3-, and 4-hydroxybenzonitriles

  芳香腈由于对人类和野生动物的健康产生有害影响，因此引起了相当大的环境问题。在本研究中，sp。据观察，菌株 BC1 能够单独利用有毒的苯甲腈和羟基苯甲腈异构体作为唯一的碳和能源。色谱和光谱分析的结果结合摄氧量和酶活性研究，揭示了苯甲腈以及2-、3-和4-羟基苯甲腈通过腈水合酶-酰胺酶代谢为相应的羧酸盐。这些羧酸盐通过中心途径进一步代谢，即菌株 BC1 中的苯甲酸盐-儿茶酚、水杨酸盐-儿茶酚、3-羟基苯甲酸盐-龙胆酸盐和 4-羟基苯甲酸盐-原儿茶素途径，最终产生 TCA 循环中间体。研究还评估了参与腈反硝化的腈水合酶和酰胺酶的底物特异性特征。此外，在菌株 BC1 中评估了由于中央代谢物诱导多个操纵子而引起的一些代谢串扰事件。本研究说明了菌株 BC1 的广泛降解潜力，具有生物技术重要性的多种分解代谢机制，首次阐明了苯甲腈和羟基苯甲腈异构体的同化途径。
• A BLOCKED POLYISOCYANATE CROSSLINKING AGENT, ITS PREPARATION METHOD AND A COATING COMPOSITION COMPRISING THE SAME
  申请人：BASF COATINGS GMBH

  公开号：US20220389153A1

  公开（公告）日：2022-12-08

  Described herein is a blocked polyisocyanate crosslinking agent obtained from reactions of components including a). at least one polyisocyanate selected from the group consisting of aliphatic polyisocyanate, cycloaliphatic polyisocyanate and polyisocyanate-functional polymer and b). at least one beta-diketone. Also described herein is a method of preparing a blocked polyisocyanate crosslinking agent as well as coating compositions including the blocked polyisocyanate crosslinking agent.
• [EN] A BLOCKED POLYISOCYANATE CROSSLINKING AGENT, ITS PREPARATION METHOD AND A COATING COMPOSITION COMPRISING THE SAME<br/>[FR] AGENT DE RÉTICULATION DE POLYISOCYANATE BLOQUÉ, SON PROCÉDÉ DE PRÉPARATION ET COMPOSITION DE REVÊTEMENT LE COMPRENANT
  申请人：BASF COATINGS GMBH

  公开号：WO2021094237A1

  公开（公告）日：2021-05-20

  This invention provides a blocked polyisocyanate crosslinking agent obtained from reactions of components comprising a). at least one polyisocyanate selected from aliphatic polyisocyanate, cycloaliphatic polyisocyanate and polyisocyanate-functional polymer and b). at least one beta-diketone. This invention also provides a method of preparing a blocked polyisocyanate crosslinking agent as well as coating compositions comprising the invented blocked polyisocyanate crosslinking agent.
• Substrate Specificity of <i>Sphingobium chlorophenolicum</i> 2,6-Dichlorohydroquinone 1,2-Dioxygenase
  作者：Timothy E. Machonkin、Amy E. Doerner

  DOI：10.1021/bi200855m

  日期：2011.10.18

  PcpA is an aromatic ring-cleaving dioxygenase that is homologous to the well-characterized Fe(II)-dependent catechol, extradiol dioxygenases. This enzyme catalyzes the oxidative cleavage of 2,6-dichlorohydroquinone in the catabolism of pentachlorophenol by Sphingobium chlorophenolicum ATCC 39723. H-1 NMR and steady-state kinetics were used to determine the regiospecificity of ring cleavage and the substrate specificity of the enzyme. PcpA exhibits a high degree of substrate specificity for 2,6-disubstituted hydroquinones, with halogens greatly preferred at those positions. Notably, the k(cat)(app)/K-mA(app) of 2,6-dichlorohydroquinone is similar to 40-fold higher than that of 2,6-dimethylhydroquinone. The asymmetric substrate 2-chloro-6-methylhydroquinone yields a mixture of 1,2- and 1,6-cleavage products. These two modes of cleavage have different K-mO(app) values (21 and 260 mu M, respectively), consistent with a mechanism in which the substrate binds in two catalytically productive orientations. In contrast, monosubstituted hydroquinones show a limited amount of ring cleavage but rapidly inactivate the enzyme in an O-2-dependent fashion, suggesting that oxidation of the Fe(II) may be the cause. Potent inhibitors of PcpA include ortho-disubstituted phenols and 3-bromocatechol. 2,6-Dibromophenol is the strongest competitive inhibitor, consistent with PcpA's substrate specificity. Several factors that could yield this specificity for halogen substituents are discussed. Interestingly, 3-bromocatechol also inactivates the enzyme, while 2,6-dihalophenols do not, indicating a requirement for two hydroxyl groups for ring cleavage and for enzyme inactivation. These results provide mechanistic insights into the hydroquinone dioxygenases.