(3E,5E)-6-羟基-2-氧代己-3,5-二烯酸 | 3270-98-2

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 中文名称: (3E,5E)-6-羟基-2-氧代己-3,5-二烯酸
• 中文别名: 环丙羧酸,2-(1E)-1-丙烯-1-基-,乙基酯
• 英文名称: 2-hydroxy-6-oxohexa-2,4-dienoic acid
• 英文别名: 2-hydroxymuconate semialdehyde；2-hydroxymuconic semi-aldehyde；2-hydroxymuconic semialdehyde；2-HMS；2-Hydroxymuconsaeuresimialdehyd
• CAS: 3270-98-2
• 化学式: C₆H₆O₄
• 分子量: 142.111
• InChiKey: KGLCZTRXNNGESL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.27
• 重原子数：
  10.0
• 可旋转键数：
  3.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  74.6
• 氢给体数：
  2.0
• 氢受体数：
  3.0

安全信息

• 海关编码：
  2918990090

反应信息

• 作为反应物：
  描述：

  (3E,5E)-6-羟基-2-氧代己-3,5-二烯酸 在 氧气 、 2-hydroxymuconic semialdehyde hydrolase 作用下， 以 aq. buffer 为溶剂， 生成 2-hydroxypenta-2,4-dienoic acid
  参考文献：
  名称：

  通过合成儿茶酚元裂解途径对木质素衍生芳烃的微生物利用

  摘要：

  木质素是来自未充分利用的植物生物质的丰富有机库。木质素的微生物利用代表了生物精炼厂的可持续方法。在这项研究中，我们基于邻苯二酚间位裂解代谢使木质素降解的芳香族化合物的生物生产多样化。为了建立有效的下游木质素分解途径，已经进行了限速原儿茶酸脱羧的瓶颈消除和酶促和代谢水平替代间位裂解途径的评估。作为碳通量指标和多功能性展示，我们设计了一条新的 1,3-BDO 合成路线，产生 0.343 gg -1来自原儿茶的产品积累。我们进一步扩展了途径以成功地将常见的解聚木质素单体异丁香酚、香草醛和香草酸同化为中心代谢物丙酮酸和乙酰辅酶 A，正如这些芳香族单体中高达 0.153 gg -1柠檬酸的生物催化所证明的那样。通过儿茶酚间位裂解建立的合成木质素分解可以作为扩展木质素利用谱的有效平台。

  DOI：

  10.1039/d1gc02347k
• 作为产物：
  描述：

  邻苯二酚 在 bleomycin resistance dioxygenase 、 zinc(II) sulfate 作用下， 以 aq. phosphate buffer 为溶剂， 生成 (3E,5E)-6-羟基-2-氧代己-3,5-二烯酸
  参考文献：
  名称：

  新分离的烃降解博来霉素抗性双加氧酶的表达，纯化，鉴定和计算机分析。

  摘要：

  在本研究中，我们报告了一种新型的博来霉素抗性双加氧酶（BRPD）的克隆，表达，纯化和表征。使用Ni-NTA亲和层析将带有组氨酸标签的融合蛋白纯化至同质，从600 ml的大肠杆菌培养物中得到1.2 mg的BRPD，比活性为6.25 U mg-1。纯化的酶是二聚体，在SDS-PAGE中分子量约为26 kDa，在天然PAGE分析中分子量约为73 kDa。通过分光光度法对酶促反应进行表征，该蛋白在金属离子存在下催化了包括邻苯二酚和对苯二酚在内的烃类底物的分解。使用EMSA凝胶阻滞分析法证明了博来霉素结合，并通过计算机分析进一步确定了推定的博来霉素结合位点。分子动力学模拟表明，在存在Fe2 +离子的情况下，BRPD达到八面体构型，形成六个配位络合物以降解类似氢醌的分子。相反，在存在Zn 2+离子的情况下，BRPD采用四面体构型，从而能够降解儿茶酚样分子。

  DOI：

  10.1007/s11033-019-05159-x

文献信息

• Molecular-Simulation-Assisted Immobilization and Catalytic Performance of CC Hydrolase MfphA on SBA-15 Mesoporous Silica
  作者：Hao Zhou、Yuanyuan Qu、Yibin Bu、Xinliang Li、Chunlei Kong、Qiao Ma、Qiang Zhang、Xuwang Zhang、Jiti Zhou

  DOI：10.1002/cplu.201100041

  日期：2012.4

  electrostatic potential calculations has been proposed to assist the immobilization process of a CC hydrolase MfphA onto mesoporous SBA‐15. The size of the enzyme, pH‐dependence of the immobilization process, and possible orientation of MfphA onto mesoporous materials (MPs) were predicted by molecular simulation. The adsorption of MfphA onto SBA‐15 reached equilibrium in 1.5 hours at pH 7.0 and the maximum

  根据同源建模和静电势计算分子模拟战略已经提出，以协助C的固定化过程 Ç水解MfphA到介孔SBA-15。通过分子模拟预测了酶的大小，固定过程的pH依赖性以及MfphA在中孔材料（MPs）上的可能取向。在pH值为7.0的1.5小时内，MfphA在SBA-15上的吸附达到平衡，最大负载量为34 mg g -1。同时在pH 9.0下，在12小时后未观察到明显的吸附，这与分子模拟预测相符。还表明，固定化后，固定化的MfphA的催化活性有所降低，但热稳定性显着提高。氯化胍（GdmCl）对固定化酶和游离酶均表现出相似的活性衰减。相比之下，固定化的MfphA在高浓度下对尿素的抵抗力要强于游离酶。同时，再循环实验表明，固定的酶在十个反应循环后保留了其初始活性的30％。
• Catalytic transformation of HODAs using an efficient meta-cleavage product hydrolase-spore surface display system
  作者：Yuanyuan Qu、Jingwei Wang、Zhaojing Zhang、Shengnan Shi、Duanxing Li、Wenli Shen、E. Shen、Jiti Zhou

  DOI：10.1016/j.molcatb.2014.02.014

  日期：2014.4
• Single Turnover Reveals Oxygenated Intermediates in Toluene/<i>o</i>-Xylene Monooxygenase in the Presence of the Native Redox Partners
  作者：Alexandria Deliz Liang、Stephen J. Lippard

  DOI：10.1021/jacs.5b07055

  日期：2015.8.26

  Toluene/o-xylene monooxygenase (ToMO) is a non-heme diiron protein that activates O-2 for subsequent arene oxidation. ToMO utilizes four protein components, a catalytic hydroxylase, a regulatory protein, a Rieske protein, and a reductase. O-2 activation and substrate hydroxylation in the presence of all four protein components is examined. These studies demonstrate the importance of native reductants by revealing reactivity unobserved when dithionite and mediators are used as the reductant. This reactivity is compared with that of other O-2-activating diiron enzymes.
• High-throughput assay of tyrosine phenol-lyase activity using a cascade of enzymatic reactions
  作者：Hang-Qin Zhu、Wen-Ye Hu、Xiao-Ling Tang、Ren-Chao Zheng、Yu-Guo Zheng

  DOI：10.1016/j.ab.2022.114547

  日期：2022.3
• Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism
  作者：Ian Davis、Yu Yang、Daniel Wherritt、Aimin Liu

  DOI：10.1074/jbc.ra118.003320

  日期：2018.6

  The kynurenine pathway is the primary route for l-tryptophan degradation in mammals. Intermediates and side products of this pathway are involved in immune response and neurodegenerative diseases. This makes the study of enzymes, especially those from mammalian sources, of the kynurenine pathway worthwhile. Recent studies on a bacterial version of an enzyme of this pathway, 2-aminomuconate semialdehyde (2-AMS) dehydrogenase (AMSDH), have provided a detailed understanding of the catalytic mechanism and identified residues conserved for muconate semialdehyde recognition and activation. Findings from the bacterial enzyme have prompted the reconsideration of the function of a previously identified human aldehyde dehydrogenase, ALDH8A1 (or ALDH12), which was annotated as a retinal dehydrogenase based on its ability to preferentially oxidize 9-cis-retinal over trans-retinal. Here, we provide compelling bioinformatics and experimental evidence that human ALDH8A1 should be reassigned to the missing 2-AMS dehydrogenase of the kynurenine metabolic pathway. For the first time, the product of the semialdehyde oxidation by AMSDH is also revealed by NMR and high-resolution MS. We found that ALDH8A1 catalyzes the NAD(+)-dependent oxidation of 2-AMS with a catalytic efficiency equivalent to that of AMSDH from the bacterium Pseudomonas fluorescens. Substitution of active-site residues required for substrate recognition, binding, and isomerization in the bacterial enzyme resulted in human ALDH8A1 variants with 160-fold increased K-m or no detectable activity. In conclusion, this molecular study establishes an additional enzymatic step in an important human pathway for tryptophan catabolism.