(3S,4R)-3,4-Dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羟基酸及其衍生物
• 英文名称: (3S,4R)-3,4-Dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate
• 化学式: C8H6O6-2
• 分子量: 198.13
• InChiKey: UKFMEOHAOCKDOL-YLWLKBPMSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  14
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  121
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (3S,4R)-3,4-Dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate 、 nicotinamide adenine dinucleotide 生成 protocatechuate 、 二氧化碳 、 NADH
  参考文献：
  名称：

  Characterization of the Terephthalate Degradation Genes of Comamonas sp. Strain E6

  摘要：

  摘要 我们分离了 Comamonas 菌株 E6，该菌株通过原儿茶酸盐（PCA）4,5-裂解途径利用对苯二甲酸盐（TPA）作为唯一的碳和能量来源。两个几乎相同的 TPA 降解基因簇、 tphR I C I A2 I A3 I B I A1 I 和 tphR II C II A2 II A3 II B II A1 II 从该菌株中分离出了根据氨基酸序列相似性，基因 tphR , tphC , tphA2 , tphA3 , tphB 和 tphA1 分别编码 IclR 型转录调节因子、质外 TPA 结合受体、TPA 1,2-二氧合酶（TPADO）加氧酶组分的大亚基、TPADO 加氧酶组分的小亚基、1,2-二羟基-3,5-环己二烯-1,4-二羧酸盐（DCD）脱氢酶和 TPADO 还原酶组分。E6 在 TPA 上的生长不受破坏 tphA2 I 或 tphA2 II 单个使用；但 tphA2 I tphA2 II 双突变体不再在 TPA 上生长，这表明两个 TPADO 基因都参与了 TPA 的降解。将携带 tphR II C II A2 II A3 II B II A1 II 赋予 Comamonas testosteroni IAM 1152 可在 PCA 上生长，但不能在 TPA 上生长。中断 tphR II 或 tphC II 这表明，这些基因是 E6 中将 TPA 转化为 PCA 的必要基因。基因 tphA1 II , tphA2 II , tphA3 和 和 tphB II 在 大肠杆菌中表达 和TphB II的细胞提取物。 II , TphA2 II 和 TphA3 II 在 NADPH 存在下将 TPA 转化为一种产物，该产物通过 TphB II .在这些结果的基础上，人们强烈认为 TPADO 是一种由末端加氧酶成分（TphA2 和 TphA3）和还原酶成分（TphA1）组成的双组分二加氧酶，而 tphB 编码为 DCD 脱氢酶。

  DOI：

  10.1128/aem.72.3.1825-1832.2006
• 作为产物：
  描述：

  氢(+1)阳离子 、 NADH 、 氧气 、 对苯二甲酸酯(2-) 生成 (3S,4R)-3,4-Dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate 、 nicotinamide adenine dinucleotide
  参考文献：
  名称：

  Enzymatic Properties of Terephthalate 1,2-Dioxygenase ofComamonassp. Strain E6

  摘要：

  Comamonas sp. E6的tphA1 II和tphA2 II A3 II基因可能编码对苯二甲酸（TPA）1,2-双加氧酶（TPADO）。为了鉴定E6 TPADO的特性，这些基因在大肠杆菌中以His标签的形式表达，并纯化了重组蛋白。TPADO活性由TphA1II和TphA2II A3 II重组，表明TPADO由还原酶（TphA1II）和末端加氧酶成分（TphA2II和TphA3II）组成。TphA1II含有FAD，并存在植物型[2Fe-2S]簇。这些结果表明TPADO是一种IB类芳香环羟基化双加氧酶。NADH和NADPH是TphA1II的有效电子供体，但根据动力学参数，NADPH似乎是生理电子供体。TPADO仅对TPA表现出活性，并且需要Fe2+。TPA的Km值和V max分别确定为72±6 μm和9.87±0.06 U/mg。

  DOI：

  10.1271/bbb.80236

文献信息

• Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component
  作者：H R Schläfli、M A Weiss、T Leisinger、A M Cook

  DOI：10.1128/jb.176.21.6644-6652.1994

  日期：1994.11

  addition of Fe2+. In the presence of O2, NADH, and fraction R, component Z catalyzed the stoichiometric transformation of TER to PC, with the intermediate formation of DCD. The reaction was confirmed as a dioxygenation when we observed incorporation of two oxygen atoms from 18O2 into PC. The substrate range of TERDOS appeared to be narrow; apart from TER, only 2,5-dicarboxypyridine and 1,4-dicarboxynaphthalene

  在对苯二甲酸（TER）-盐培养基中生长的Comamonas testosteroni T-2合成可诱导的酶，该酶将TER转化为（1R，2S）-二羟基-3,5-环己二烯-1,4-二羧酸（DCD）和原儿茶酸酯（PC ）。细胞提取物的阴离子交换色谱法产生了两组馏分R和Z，这是将TER氧化为DCD所必需的。我们将这种活性称为TER双加氧酶系统（TERDOS）。将DCD转换为PC的NAD（+）依赖性DCD脱氢酶与所有馏分R重叠。没有从馏分R中获得明显的纯化，该馏分R包含TERDOS的NADH依赖性还原酶功能。在梯度结束时，馏分Z基本包含一种蛋白质，可通过疏水相互作用色谱法进一步纯化。这个分量Z 具有Rieske [2Fe-2S]蛋白的紫外可见光谱和电子顺磁共振特征，被认为是加氧酶。在天然条件下观察到加氧酶Z的M（r）约为126,000。加氧酶Z由两个亚基α和β组成，在变性条件下，M（r）分别为49,000和18
• Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D.
  作者：Y Z Wang、Y Zhou、G J Zylstra

  DOI：10.1289/ehp.95103s49

  日期：1995.6

  Comamonas testosteroni YZW-D was isolated from Passaic River sediment for its ability to degrade isophthalate and terephthalate. Degradation of the two isomeric compounds proceeds via separately inducible catabolic pathways that converge at protocatechuate. Analysis of the catabolic pathways by which these two isomers are degraded demonstrated that a cis-dihydrodiol intermediate is involved in both pathways. The genes for the conversion of isophthalate and terephthalate to protocatechuate were cloned on a single fragment of genomic DNA from C. testosteroni YZW-D. The two operons were located by subcloning and mutant complementation experiments. The regions coding for the two degradative pathways were sequenced. Analysis of the nucleotide sequence for the isophthalate degradation operon located genes for a dioxygenase, a transport protein, a cis-dihydrodiol dehydrogenase, and a reductase. Analysis of the nucleotide sequence for the terephthalate degradation operon located genes for a regulatory protein, a transport protein, a dioxygenase large subunit, a dioxygenase small subunit, a cis-dihydrodiol dehydrogenase, and a reductase.
• Enzymatic Properties of Terephthalate 1,2-Dioxygenase of<i>Comamonas</i>sp. Strain E6
  作者：Yuki FUKUHARA、Daisuke KASAI、Yoshihiro KATAYAMA、Masao FUKUDA、Eiji MASAI

  DOI：10.1271/bbb.80236

  日期：2008.9.23

  The tphA1  II and tphA2  II  A3  II genes of Comamonas sp. E6 perhaps code for the terephthalate (TPA) 1,2-dioxygenase (TPADO). To characterize E6 TPADO, these genes were expressed in a His-tagged form in Escherichia coli, and the recombinant proteins were purified. TPADO activity was reconstituted from TphA1II and TphA2IIA3II, indicating that TPADO consists of a reductase (TphA1II) and a terminal oxygenase component (TphA2II and TphA3II). TphA1II contains FAD, and the presence of a plant-type [2Fe-2S] cluster was suggested. These results indicate that TPADO is a class IB aromatic ring-hydroxylating dioxygenase. NADH and NADPH were effective as electron donors for TphA1II, but NADPH appeared to be the physiological electron donor, based on the kinetic parameters. TPADO showed activity only toward TPA, and Fe2+ was required for it. The Km values for TPA and the V  max were determined to be 72±6 μm and 9.87±0.06 U/mg respectively.

  Comamonas sp. E6的tphA1 II和tphA2 II A3 II基因可能编码对苯二甲酸（TPA）1,2-双加氧酶（TPADO）。为了鉴定E6 TPADO的特性，这些基因在大肠杆菌中以His标签的形式表达，并纯化了重组蛋白。TPADO活性由TphA1II和TphA2II A3 II重组，表明TPADO由还原酶（TphA1II）和末端加氧酶成分（TphA2II和TphA3II）组成。TphA1II含有FAD，并存在植物型[2Fe-2S]簇。这些结果表明TPADO是一种IB类芳香环羟基化双加氧酶。NADH和NADPH是TphA1II的有效电子供体，但根据动力学参数，NADPH似乎是生理电子供体。TPADO仅对TPA表现出活性，并且需要Fe2+。TPA的Km值和V max分别确定为72±6 μm和9.87±0.06 U/mg。
• Characterization of the Terephthalate Degradation Genes of <i>Comamonas</i> sp. Strain E6
  作者：Mikio Sasoh、Eiji Masai、Satoko Ishibashi、Hirofumi Hara、Naofumi Kamimura、Keisuke Miyauchi、Masao Fukuda

  DOI：10.1128/aem.72.3.1825-1832.2006

  日期：2006.3

  We isolated Comamonas sp. strain E6, which utilizes terephthalate (TPA) as the sole carbon and energy source via the protocatechuate (PCA) 4,5-cleavage pathway. Two almost identical TPA degradation gene clusters, tphR _I C _I A2 _I A3 _I B _I A1 _I and tphR _II C _II A2 _II A3 _II B _II A1 _II , were isolated from this strain. Based on amino acid sequence similarity, the genes tphR , tphC , tphA2 , tphA3 , tphB , and tphA1 were predicted to code, respectively, for an IclR-type transcriptional regulator, a periplasmic TPA binding receptor, the large subunit of the oxygenase component of TPA 1,2-dioxygenase (TPADO), the small subunit of the oxygenase component of TPADO, a 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate (DCD) dehydrogenase, and a reductase component of TPADO. The growth of E6 on TPA was not affected by disruption of either tphA2 _I or tphA2 _II singly; however, the tphA2 _I tphA2 _II double mutant no longer grew on TPA, suggesting that both TPADO genes are involved in TPA degradation. Introduction of a plasmid carrying tphR _II C _II A2 _II A3 _II B _II A1 _II conferred the TPA utilization phenotype on Comamonas testosteroni IAM 1152, which is able to grow on PCA but not on TPA. Disruption of either tphR _II or tphC _II on this plasmid resulted in the loss of the growth of IAM 1152 on TPA, suggesting that these genes are essential to convert TPA to PCA in E6. The genes tphA1 _II , tphA2 _II , tphA3 _II , and tphB _II were expressed in Escherichia coli , and the resultant cell extracts containing TphA1 _II , TphA2 _II , and TphA3 _II converted TPA in the presence of NADPH into a product which was transformed to PCA by TphB _II . On the basis of these results, TPADO was strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase (TphA1), and tphB codes for the DCD dehydrogenase.

  摘要 我们分离了 Comamonas 菌株 E6，该菌株通过原儿茶酸盐（PCA）4,5-裂解途径利用对苯二甲酸盐（TPA）作为唯一的碳和能量来源。两个几乎相同的 TPA 降解基因簇、 tphR I C I A2 I A3 I B I A1 I 和 tphR II C II A2 II A3 II B II A1 II 从该菌株中分离出了根据氨基酸序列相似性，基因 tphR , tphC , tphA2 , tphA3 , tphB 和 tphA1 分别编码 IclR 型转录调节因子、质外 TPA 结合受体、TPA 1,2-二氧合酶（TPADO）加氧酶组分的大亚基、TPADO 加氧酶组分的小亚基、1,2-二羟基-3,5-环己二烯-1,4-二羧酸盐（DCD）脱氢酶和 TPADO 还原酶组分。E6 在 TPA 上的生长不受破坏 tphA2 I 或 tphA2 II 单个使用；但 tphA2 I tphA2 II 双突变体不再在 TPA 上生长，这表明两个 TPADO 基因都参与了 TPA 的降解。将携带 tphR II C II A2 II A3 II B II A1 II 赋予 Comamonas testosteroni IAM 1152 可在 PCA 上生长，但不能在 TPA 上生长。中断 tphR II 或 tphC II 这表明，这些基因是 E6 中将 TPA 转化为 PCA 的必要基因。基因 tphA1 II , tphA2 II , tphA3 和 和 tphB II 在 大肠杆菌中表达 和TphB II的细胞提取物。 II , TphA2 II 和 TphA3 II 在 NADPH 存在下将 TPA 转化为一种产物，该产物通过 TphB II .在这些结果的基础上，人们强烈认为 TPADO 是一种由末端加氧酶成分（TphA2 和 TphA3）和还原酶成分（TphA1）组成的双组分二加氧酶，而 tphB 编码为 DCD 脱氢酶。