1-monoenoyl-CoA | 6420-00-4

• 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: 1-monoenoyl-CoA
• 英文别名: monoenoyl-CoA；cyclohex-1-ene-1-carboxyl-CoA；Cyclohex-1-ene-1-carbonyl-CoA；S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] cyclohexene-1-carbothioate
• CAS: 6420-00-4
• 化学式: C₂₈H₄₄N₇O₁₇P₃S
• 分子量: 875.681
• InChiKey: YTTZSBMCHSFQSJ-TYHXJLICSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.7
• 重原子数：
  56
• 可旋转键数：
  21
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  389
• 氢给体数：
  9
• 氢受体数：
  22

反应信息

• 作为反应物：
  描述：

  1-monoenoyl-CoA 在 3-吗啉丙磺酸 、 titanium(III) citrate 、 7,8-dihydro-2,12-dimethyl-6H-dipyrido[1,2-a:2',1'-c][1,4]diazepinediium dibromide 、 sodium chloride 、 potassium hydroxide 、 magnesium chloride 作用下， 反应 0.01h， 生成 环己烷羧基-辅酶A
  参考文献：
  名称：

  Reversible Biological Birch Reduction at an Extremely Low Redox Potential

  摘要：

  The Birch reduction of aromatic rings to cyclohexadiene compounds is widely used in chemical synthesis and requires solvated electrons, the most potent reductants known in organic chemistry. Benzoyl-coenzyme A (CoA) reductases (BCR) are key enzymes in the anaerobic bacterial degradation of aromatic compounds and catalyze an analogous reaction under physiological conditions. Class I BCRs are FeS enzymes and couple the reductive dearomatization of benzoyl-CoA to cyclohexa-1,5-diene-1-carboxyl-CoA (dienoyl-CoA) to a stoichiometric ATP hydrolysis. Here, we report on a tungsten-containing class II BCR from Geobacter metallireducens that catalyzed the fully reversible, ATP-independent dearomatization of benzoyl-CoA to dienoyl-CoA. BCR additionally catalyzed the disproportionation of dienoyl-CoA to benzoyl-CoA/monoenoyl-CoA and the four- and six-electron reduction of benzoyl-CoA in the presence of a reduced low-potential bridged 2,2'-bipyridyl redox dye. Reversible redox titration experiments in the presence of this redox dye revealed a midpoint potential of E-0'= -622 mV for the benzoyl-CoA/dienoyl-CoA couple, which is far below the values of other known reversible substrate/product redox couples in enzymology. This work demonstrates the efficiency of reversible metalloenzyme catalysis, which in chemical synthesis can only be achieved under essentially irreversible conditions.

  DOI：

  10.1021/ja103448u
• 作为产物：
  描述：

  1,5-dienoyl-CoA 在 3-吗啉丙磺酸 、 titanium(III) citrate 、 7,8-dihydro-2,12-dimethyl-6H-dipyrido[1,2-a:2',1'-c][1,4]diazepinediium dibromide 、 sodium chloride 、 potassium hydroxide 、 magnesium chloride 作用下， 反应 0.01h， 以25%的产率得到1-monoenoyl-CoA
  参考文献：
  名称：

  Reversible Biological Birch Reduction at an Extremely Low Redox Potential

  摘要：

  The Birch reduction of aromatic rings to cyclohexadiene compounds is widely used in chemical synthesis and requires solvated electrons, the most potent reductants known in organic chemistry. Benzoyl-coenzyme A (CoA) reductases (BCR) are key enzymes in the anaerobic bacterial degradation of aromatic compounds and catalyze an analogous reaction under physiological conditions. Class I BCRs are FeS enzymes and couple the reductive dearomatization of benzoyl-CoA to cyclohexa-1,5-diene-1-carboxyl-CoA (dienoyl-CoA) to a stoichiometric ATP hydrolysis. Here, we report on a tungsten-containing class II BCR from Geobacter metallireducens that catalyzed the fully reversible, ATP-independent dearomatization of benzoyl-CoA to dienoyl-CoA. BCR additionally catalyzed the disproportionation of dienoyl-CoA to benzoyl-CoA/monoenoyl-CoA and the four- and six-electron reduction of benzoyl-CoA in the presence of a reduced low-potential bridged 2,2'-bipyridyl redox dye. Reversible redox titration experiments in the presence of this redox dye revealed a midpoint potential of E-0'= -622 mV for the benzoyl-CoA/dienoyl-CoA couple, which is far below the values of other known reversible substrate/product redox couples in enzymology. This work demonstrates the efficiency of reversible metalloenzyme catalysis, which in chemical synthesis can only be achieved under essentially irreversible conditions.

  DOI：

  10.1021/ja103448u

文献信息

• A Pair of Atypical KAS III Homologues with Initiation and Elongation Functions Program the Polyketide Biosynthesis in Asukamycin
  作者：Xiaoli Yan、Jun Zhang、Hongqun Tan、Zhihao Liu、Kai Jiang、Wenya Tian、Mengmeng Zheng、Zhi Lin、Zixin Deng、Xudong Qu

  DOI：10.1002/anie.202200879

  日期：2022.5.2

  KAS IIIs are known to be involved in the initiation step of polyketide and fatty acid biosynthesis. In vitro reconstitution of the upper triene chain of asukamycin unveils two highly unusual KAS IIIs which both exhibit initiation and iterative elongation activity. Together with the permissive ketoreductase and dehydratase, these C−C bond-forming enzymes can synthesize a large variety of polyenes.

  已知 KAS III 参与聚酮化合物和脂肪酸生物合成的起始步骤。Asukamycin 上三烯链的体外重组揭示了两种非常不寻常的 KAS III，它们都表现出起始和迭代延伸活性。与允许的酮还原酶和脱水酶一起，这些 C-C 键形成酶可以合成多种多烯。
• Reversible Biological Birch Reduction at an Extremely Low Redox Potential
  作者：Johannes W. Kung、Sven Baumann、Martin von Bergen、Michael Müller、Peter-Leon Hagedoorn、Wilfred R. Hagen、Matthias Boll

  DOI：10.1021/ja103448u

  日期：2010.7.21

  The Birch reduction of aromatic rings to cyclohexadiene compounds is widely used in chemical synthesis and requires solvated electrons, the most potent reductants known in organic chemistry. Benzoyl-coenzyme A (CoA) reductases (BCR) are key enzymes in the anaerobic bacterial degradation of aromatic compounds and catalyze an analogous reaction under physiological conditions. Class I BCRs are FeS enzymes and couple the reductive dearomatization of benzoyl-CoA to cyclohexa-1,5-diene-1-carboxyl-CoA (dienoyl-CoA) to a stoichiometric ATP hydrolysis. Here, we report on a tungsten-containing class II BCR from Geobacter metallireducens that catalyzed the fully reversible, ATP-independent dearomatization of benzoyl-CoA to dienoyl-CoA. BCR additionally catalyzed the disproportionation of dienoyl-CoA to benzoyl-CoA/monoenoyl-CoA and the four- and six-electron reduction of benzoyl-CoA in the presence of a reduced low-potential bridged 2,2'-bipyridyl redox dye. Reversible redox titration experiments in the presence of this redox dye revealed a midpoint potential of E-0'= -622 mV for the benzoyl-CoA/dienoyl-CoA couple, which is far below the values of other known reversible substrate/product redox couples in enzymology. This work demonstrates the efficiency of reversible metalloenzyme catalysis, which in chemical synthesis can only be achieved under essentially irreversible conditions.