(2E,4E)-2,4-dichlorohexa-2,4-dienedioate

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (2E,4E)-2,4-dichlorohexa-2,4-dienedioate
• 化学式: C6H2Cl2O4-2
• 分子量: 208.98
• InChiKey: FHXOPKKNGKBBKG-DXLKSGPOSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  12
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  80.3
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  2,4-Dichloro-5-oxo-2,5-dihydro-2-furylacetate 生成 (2E,4E)-2,4-dichlorohexa-2,4-dienedioate 、 氢(+1)阳离子
  参考文献：
  名称：

  Kuhm A.E.; Schlomann M.; Knackmuss H.J., Biochem J, 1990, 0264-6021, 877-83

  摘要：

  DOI：

文献信息

• Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates
  作者：J R van der Meer、R I Eggen、A J Zehnder、W M de Vos

  DOI：10.1128/jb.173.8.2425-2434.1991

  日期：1991.4

  Pseudomonas sp. strain P51 contains two gene clusters located on catabolic plasmid pP51 that encode the degradation of chlorinated benzenes. The nucleotide sequence of a 5,499-bp region containing the chlorocatechol-oxidative gene cluster tcbCDEF was determined. The sequence contained five large open reading frames, which were all colinear. The functionality of these open reading frames was studied with various Escherichia coli expression systems and by analysis of enzyme activities. The first gene, tcbC, encodes a 27.5-kDa protein with chlorocatechol 1,2-dioxygenase activity. The tcbC gene is followed by tcbD, which encodes cycloisomerase II (39.5 kDa); a large open reading frame (ORF3) with an unknown function; tcbE, which encodes hydrolase II (25.8 kDa); and tcbF, which encodes a putative trans-dienelactone isomerase (37.5 kDa). The tcbCDEF gene cluster showed strong DNA homology (between 57.6 and 72.1% identity) and an organization similar to that of other known plasmid-encoded operons for chlorocatechol metabolism, e.g., clcABD of Pseudomonas putida and tfdCDEF of Alcaligenes eutrophus JMP134. The identity between amino acid sequences of functionally related enzymes of the three operons varied between 50.6 and 75.7%, with the tcbCDEF and tfdCDEF pair being the least similar of the three. Measurements of the specific activities of chlorocatechol 1,2-dioxygenases encoded by tcbC, clcA, and tfdC suggested that a specialization among type II enzymes has taken place. TcbC preferentially converts 3,4-dichlorocatechol relative to other chlorinated catechols, whereas TfdC has a higher activity toward 3,5-dichlorocatechol. ClcA takes an intermediate position, with the highest activity level for 3-chlorocatechol and the second-highest level for 3,5-dichlorocatechol.

  Pseudomonas sp.菌株P51含有位于降解质粒pP51上的两个基因簇，编码对氯代苯降解。确定了一个5,499 bp区域的核苷酸序列，其中包含氯间苯二酚氧化基因簇tcbCDEF。序列包含五个大的开放阅读框架，它们都是共线的。用各种大肠杆菌表达系统和酶活性分析研究了这些开放阅读框架的功能。第一个基因tcbC编码一个27.5 kDa的蛋白质，具有氯间苯二酚1,2-双加氧酶活性。tcbC基因后面是tcbD，它编码环异构酶II（39.5 kDa）；一个具有未知功能的大开放阅读框架（ORF3）；tcbE，它编码水解酶II（25.8 kDa）；以及tcbF，它编码一个假定的反式二烯酸内酯酶（37.5 kDa）。tcbCDEF基因簇显示出强的DNA同源性（57.6%至72.1%的同一性）和与其他已知质粒编码的氯间苯二酚代谢操作子的组织类似性，例如Pseudomonas putida的clcABD和Alcaligenes eutrophus JMP134的tfdCDEF。三个操作子中功能相关酶的氨基酸序列之间的同一性在50.6%至75.7%之间变化，其中tcbCDEF和tfdCDEF对的相似性最小。测量由tcbC、clcA和tfdC编码的氯间苯二酚1,2-双加氧酶的特异性活性表明，类型II酶之间存在专业化。TcbC优先转化3,4-二氯间苯二酚相对于其他氯化间苯二酚，而TfdC对3,5-二氯间苯二酚的活性更高。ClcA处于中间位置，对3-氯间苯二酚具有最高的活性水平，对3,5-二氯间苯二酚具有次高的水平。
• Evolutionary Relationship between Chlorocatechol Catabolic Enzymes from <i>Rhodococcus opacus</i> 1CP and Their Counterparts in Proteobacteria: Sequence Divergence and Functional Convergence
  作者：Dirk Eulberg、Elena M. Kourbatova、Ludmila A. Golovleva、Michael Schlömann

  DOI：10.1128/jb.180.5.1082-1094.1998

  日期：1998.3

  Biochemical investigations of the muconate and chloromuconate cycloisomerases from the chlorophenol-utilizing strain Rhodococcus opacus ( erythropolis ) 1CP had previously indicated that the chlorocatechol catabolic pathway of this strain may have developed independently from the corresponding pathways of proteobacteria. To test this hypothesis, we cloned the chlorocatechol catabolic gene cluster of strain 1CP by using PCR with primers derived from sequences of N termini and peptides of purified chlorocatechol 1,2-dioxygenase and chloromuconate cycloisomerase. Sequencing of the clones revealed that they comprise different parts of the same gene cluster in which five open reading frames have been identified. The clcB gene for chloromuconate cycloisomerase is transcribed divergently from a gene which codes for a LysR-type regulatory protein, the presumed ClcR. Downstream of clcR but separated from it by 222 bp, we detected the clcA and clcD genes, which could unambiguously be assigned to chlorocatechol 1,2-dioxygenase and dienelactone hydrolase. A gene coding for a maleylacetate reductase could not be detected. Instead, the product encoded by the fifth open reading frame turned out to be homologous to transposition-related proteins of IS 1031 and Tn 4811 . Sequence comparisons of ClcA and ClcB to other 1,2-dioxygenases and cycloisomerases, respectively, clearly showed that the chlorocatechol catabolic enzymes of R. opacus 1CP represent different branches in the dendrograms than their proteobacterial counterparts. Thus, while the sequences diverged, the functional adaptation to efficient chlorocatechol metabolization occurred independently in proteobacteria and gram-positive bacteria, that is, by functionally convergent evolution.

  摘要 对氯酚利用菌株的粘液酸盐和氯琥珀酸盐环异构酶的生化研究 蛋白红球菌（Rhodococcus opacus ( erythropolis )1CP 以前曾指出，该菌株的儿茶酚代谢途径可能是独立于蛋白细菌的相应途径而发展起来的。为了验证这一假设，我们利用纯化的儿茶酚 1,2-二氧酶和氯琥珀酸环异构酶的 N 端和多肽序列为引物，通过 PCR 克隆了 1CP 菌株的儿茶酚代谢基因簇。对克隆进行测序后发现，它们由同一基因簇的不同部分组成，其中有五个开放阅读框。其中 clcB 的转录与一个编码 LysR 型调控蛋白（推测为 ClcR）的基因不同。在 下游 下游，但与之相隔 222 bp，我们检测到了 clcA 和 基因 基因，这两个基因可明确归属于儿茶酚 1,2-二氧 化酶和二内酯水解酶。未能检测到编码马来酰乙酸还原酶的基因。相反，第五个开放阅读框编码的产物与 IS 1031 和 Tn 4811 .ClcA 和 ClcB 分别与其他 1,2-二氧合酶和环异构酶的序列比较清楚地表明，岩白菜素蛙的氯邻苯二酚分解酶与其他 1,2-二氧合酶和环异构酶是同源的。 R. opacus 1CP 在树枝图中的分支与蛋白细菌的对应分支不同。因此，虽然序列出现了分化，但蛋白细菌和革兰氏阳性细菌对高效代谢儿茶酚的功能适应是独立发生的，即通过功能趋同进化实现的。
• Two Chlorocatechol Catabolic Gene Modules on Plasmid pJP4
  作者：Michael Schlömann

  DOI：10.1128/jb.184.15.4049-4053.2002

  日期：2002.8
• Kuhm A.E.; Schlomann M.; Knackmuss H.J., Biochem J, 1990, 0264-6021, 877-83
  作者：Kuhm A.E.、Schlomann M.、Knackmuss H.J.、Pieper D.H.

  DOI：——

  日期：——