Maleylacetate

• 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: Maleylacetate
• 英文别名: (Z)-4-oxohex-2-enedioate
• 化学式: C6H4O5-2
• 分子量: 156.09
• InChiKey: SOXXPQLIZIPMIZ-UPHRSURJSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  11
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  97.3
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  3-Hydroxy-cis,cis-muconate(2-) 生成 Maleylacetate
  参考文献：
  名称：

  摘要：

  DOI：

文献信息

• Pathway for Biodegradation of <i>p</i> -Nitrophenol in a <i>Moraxella</i> sp
  作者：Jim C. Spain、David T. Gibson

  DOI：10.1128/aem.57.3.812-819.1991

  日期：1991.3

  A Moraxella strain grew on p -nitrophenol with stoichiometric release of nitrite. During induction of the enzymes for growth on p -nitrophenol, traces of hydroquinone accumulated in the medium. In the presence of 2,2′-dipyridyl, p -nitrophenol was converted stoichiometrically to hydroquinone. Particulate enzymes catalyzed the conversion of p -nitrophenol to hydroquinone in the presence of NADPH and oxygen. Soluble enzymes catalyzed the conversion of hydroquinone to γ-hydroxymuconic semialdehyde, which was identified by high-performance liquid chromatography (HPLC)-mass spectroscopy. Upon addition of catalytic amounts of NAD ⁺ , γ-hydroxymuconic semialdehyde was converted to β-ketoadipic acid. In the presence of pyruvate and lactic dehydrogenase, substrate amounts of NAD were required and γ-hydroxymuconic semialdehyde was converted to maleylacetic acid, which was identified by HPLC-mass spectroscopy. Similar results were obtained when the reaction was carried out in the presence of potassium ferricyanide. Extracts prepared from p -nitrophenol-growth cells also contained an enzyme that catalyzed the oxidation of 1,2,4-benzenetriol to maleylacetic acid. The enzyme responsible for the oxidation of 1,2,4-benzenetriol was separated from the enzyme responsible for hydroquinone oxidation by DEAE-cellulose chromatography. The results indicate that the pathway for biodegradation of p -nitrophenol involves the initial removal of the nitro group as nitrite and formation of hydroquinone. 1,4-Benzoquinone, a likely intermediate in the initial reaction, was not detected. Hydroquinone is converted to β-ketoadipic acid via γ-hydroxymuconic semialdehyde and maleylacetic acid.

  一株Moraxella菌株能够在p-硝基酚上生长，并释放亚硝酸。在诱导生长p-硝基酚的酶时，培养基中积累了少量的对苯二酚。在存在2,2'-联吡啶的情况下，p-硝基酚被定量地转化为对苯二酚。颗粒酶在NADPH和氧气的存在下催化p-硝基酚转化为对苯二酚。可溶性酶催化对苯二酚转化为γ-羟基须亚醛，并通过高效液相色谱（HPLC）-质谱分析鉴定。在添加催化量的NAD+时，γ-羟基须亚醛被转化为β-酮基己二酸。在丙酮酸和乳酸脱氢酶的存在下，需要底物量的NAD，并且γ-羟基须亚醛被转化为马来酰乙酸，通过HPLC-质谱分析鉴定。在存在高锰酸钾的情况下进行反应，得到类似的结果。从p-硝基酚生长细胞中制备的提取物也含有一种酶，能催化1,2,4-苯三酚氧化为马来酰乙酸。通过DEAE-纤维素柱层析将负责1,2,4-苯三酚氧化的酶与负责对苯二酚氧化的酶分离开来。结果表明，p-硝基酚的生物降解途径涉及最初将硝基去除为亚硝酸并形成对苯二酚。初步反应中可能存在的1,4-苯醌未被检测到。对苯二酚通过γ-羟基须亚醛和马来酰乙酸转化为β-酮基己二酸。
• Cloning and Sequencing of a Novel <i>meta</i> -Cleavage Dioxygenase Gene Whose Product Is Involved in Degradation of γ-Hexachlorocyclohexane in <i>Sphingomonas paucimobilis</i>
  作者：Keisuke Miyauchi、Yugo Adachi、Yuji Nagata、Masamichi Takagi

  DOI：10.1128/jb.181.21.6712-6719.1999

  日期：1999.11

  Sphingomonas (formerly Pseudomonas ) paucimobilis UT26 utilizes γ-hexachlorocyclohexane (γ-HCH), a halogenated organic insecticide, as a sole source of carbon and energy. In a previous study, we showed that γ-HCH is degraded to chlorohydroquinone (CHQ) and then to hydroquinone (HQ), although the rate of reaction from CHQ to HQ was slow (K. Miyauchi, S. K. Suh, Y. Nagata, and M. Takagi, J. Bacteriol. 180:1354–1359, 1998). In this study, we cloned and characterized a gene, designated linE , which is located upstream of linD and is directly involved in the degradation of CHQ. The LinE protein consists of 321 amino acids, and all of the amino acids which are reported to be essential for the activity of meta -cleavage dioxygenases are conserved in LinE. Escherichia coli overproducing LinE could convert both CHQ and HQ, producing γ-hydroxymuconic semialdehyde and maleylacetate, respectively, with consumption of O ₂ but could not convert catechol, which is one of the major substrates for meta -cleavage dioxygenases. LinE seems to be resistant to the acylchloride, which is the ring cleavage product of CHQ and which seems to react with water to be converted to maleylacetate. These results indicated that LinE is a novel type of meta -cleavage dioxygenase, designated (chloro)hydroquinone 1,2-dioxygenase, which cleaves aromatic rings with two hydroxyl groups at para positions preferably. This study represents a direct demonstration of a new type of ring cleavage pathway for aromatic compounds, the hydroquinone pathway.

  摘要 鞘氨醇单胞菌 （原 假单胞菌 ) paucimobilis UT26利用卤代有机杀虫剂γ-六氯环己烷（γ-HCH）作为唯一的碳和能量来源。在之前的一项研究中，我们发现γ-HCH 被降解为氯氢醌（CHQ），然后再降解为对苯二酚（HQ），尽管从 CHQ 到 HQ 的反应速度很慢（K. Miyauchi, S. K. Suh, Y. Nagata, and M. Takagi, J. Bacteriol.180:1354-1359, 1998).在本研究中，我们克隆并鉴定了一个基因，命名为 linE 位于 linD 该基因直接参与了 CHQ 的降解。LinE蛋白由321个氨基酸组成，其中所有的氨基酸都是报道的meta-CHQ降解过程中所必需的。 元 -清除二氧酶活性所必需的氨基酸在 LinE 中都是保守的。 大肠杆菌 过量产生 LinE 的大肠杆菌可同时转化 CHQ 和 HQ，在消耗 O 2 但不能转化儿茶酚，而儿茶酚是 元 -二氧酶的主要底物之一。LinE 似乎对酰基氯有抵抗力，酰基氯是 CHQ 的环裂解产物，似乎会与水反应转化为马来乙酸酯。这些结果表明，LinE 是一种新型的 元 -对苯二酚 1,2-二氧 化酶，它能裂解带有两个羟基的芳香环。 对位 位置上有两个羟基的芳香环。这项研究直接证明了一种新型的芳香化合物环裂解途径--对苯二酚途径。
• Identification and Characterization of Genes Involved in the Downstream Degradation Pathway of γ-Hexachlorocyclohexane in <i>Sphingomonas paucimobilis</i> UT26
  作者：Ryo Endo、Mayuko Kamakura、Keisuke Miyauchi、Masao Fukuda、Yoshiyuki Ohtsubo、Masataka Tsuda、Yuji Nagata

  DOI：10.1128/jb.187.3.847-853.2005

  日期：2005.2

  Sphingomonas paucimobilis UT26 utilizes γ-hexachlorocyclohexane (γ-HCH) as a sole source of carbon and energy. In our previous study, we cloned and characterized genes that are involved in the conversion of γ-HCH to maleylacetate (MA) via chlorohydroquinone (CHQ) in UT26. In this study, we identified and characterized an MA reductase gene, designated linF , that is essential for the utilization of γ-HCH in UT26. A gene named linEb , whose deduced product showed significant identity to LinE (53%), was located close to linF . LinE is a novel type of ring cleavage dioxygenase that catalyzes the conversion of CHQ to MA. LinEb expressed in Escherichia coli transformed CHQ and 2,6-dichlorohydroquinone to MA and 2-chloromaleylacetate, respectively. Our previous and present results indicate that UT26 (i) has two gene clusters for degradation of chlorinated aromatic compounds via hydroquinone-type intermediates and (ii) uses at least parts of both clusters for γ-HCH utilization.

  摘要 Sphingomonas paucimobilis UT26利用γ-六氯环己烷（γ-HCH）作为唯一的碳和能量来源。在之前的研究中，我们克隆并鉴定了UT26中参与将γ-HCH通过氯氢醌（CHQ）转化为马来乙酸酯（MA）的基因。在这项研究中，我们发现并鉴定了一个 MA 还原酶基因，命名为 linF 该基因对UT26中γ-HCH的利用至关重要。一个名为 linEb 的基因，其推导产物与 LinE 有显著的相似性（53%），该基因位于靠近 linF .LinE 是一种新型的裂环二氧酶，可催化 CHQ 向 MA 的转化。LinEb 在 大肠杆菌 将 CHQ 和 2,6-二氯对苯二酚分别转化为 MA 和 2-氯马来酰乙酸酯。我们之前和现在的研究结果表明，UT26 (i) 有两个基因簇，可通过对苯二酚型中间体降解氯化芳香族化合物，(ii) 至少使用这两个基因簇的部分基因利用γ-HCH。
• Maleylacetate reductase from <i>Trichosporon cutaneum</i>
  作者：A B Gaal、H Y Neujahr

  DOI：10.1042/bj1850783

  日期：1980.3.1

  The enzyme catalysing the reduction of maleylacetate to 3-oxoadipate was purified 150-fold from Trichosporon cutaneum, induced for aromatic metabolisms by growth with resorcinol as a major carbon source. The enzyme separated upon electrofocusing into three species with PI values 4.6, 5.1 and 5.6. They had similar catalytic properties and the same molecular weight.

  该酶催化将马来酰乙酸还原为3-氧代己二酸，从通过使用间苯二酚作为主要碳源诱导芽孢链霉菌的芳香代谢中纯化了150倍。该酶在电泳分离中分为三个物种，其等电点分别为4.6、5.1和5.6。它们具有相似的催化性质和相同的分子量。
• Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)
  作者：V Seibert、K Stadler-Fritzsche、M Schlömann

  DOI：10.1128/jb.175.21.6745-6754.1993

  日期：1993.11

  Maleylacetate reductase (EC 1.3.1.32) plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. The enzyme was purified to apparent homogeneity from an extract of 2,4-dichlorophenoxyacetate (2,4-D)-grown cells of Alcaligenes eutrophus JMP134. Maleylacetate reductase appears to be a dimer of two identical subunits of 35 kDa. The pI was determined to be at pH 5.4. There was no indication of a flavin prosthetic group. The enzyme was inactivated by p-chloromercuribenzoate but not by EDTA, 1,10-phenanthroline, or dithiothreitol. Maleylacetate and 2-chloromaleylacetate were converted with similar efficiencies (with NADH as cosubstrate, Km = 31 microM for each substrate and kcat = 8,785 and 7,280/min, respectively). NADH was preferred to NADPH as the cosubstrate. Upon reduction of 2-chloramaleylacetate by the purified enzyme, chloride was liberated and the resulting maleylacetate was further reduced by a second NADH. These results and the kinetic parameters suggest that the maleylacetate reductase is sufficient to channel the 2,4-D degradation intermediate 2-chloromaleylacetate into the 3-oxoadipate pathway. In a data base search the NH2-terminal sequence of maleylacetate reductase was found to be most similar to that of TfdF, a pJP4-encoded protein of as-yet-unknown function in 2,4-D degradation.

  Maleylacetate还原酶（EC 1.3.1.32）在氯芳烃化合物的降解中起着重要作用，将Maleylacetate及其一些取代衍生物引导到3-氧基己二酸途径中。该酶从Alcaligenes eutrophus JMP134的2,4-二氯苯氧乙酸（2,4-D）培养细胞提取物中纯化得到，表观纯度较高。Maleylacetate还原酶似乎是两个相同亚基的二聚体，每个亚基的分子量为35kDa。其等电点pH值为5.4。没有迹象表明存在黄酮辅基。该酶被对氯汞苯甲酸酯失活，但不被EDTA、1,10-邻菲啰啉或二硫苏糖醇所失活。Maleylacetate和2-氯maleylacetate的转化效率相似（以NADH为共底物，每个底物的Km值为31微米，kcat分别为8,785和7,280/分钟）。NADH优先于NADPH作为共底物。通过纯化酶对2-氯maleylacetate的还原，释放氯离子，生成的maleylacetate又被第二个NADH进一步还原。这些结果和动力学参数表明，maleylacetate还原酶足以将2,4-D降解中间体2-氯maleylacetate引导到3-氧基己二酸途径中。在数据库搜索中，发现maleylacetate还原酶的NH2端序列与TfdF最为相似，后者是2,4-D降解中尚未知功能的pJP4编码蛋白。