pentanoyl coenzyme A | 4752-33-4

• 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: pentanoyl coenzyme A
• 英文别名: Pentanoyl-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] pentanethioate
• CAS: 4752-33-4
• 化学式: C₂₆H₄₄N₇O₁₇P₃S
• 分子量: 851.659
• InChiKey: RXUATCUKICAIOA-ZMHDXICWSA-N

物化性质

• 密度：
  1.79±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  54
• 可旋转键数：
  23
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.69
• 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：

  pentanoyl coenzyme A 在 mitochondrial acyl-coenzyme A hydrolase from rat liver 、 水 、 三羟甲基氨基甲烷盐酸盐 作用下， 生成 辅酶 A
  参考文献：
  名称：

  溶剂衍生的草酸的CoA酯的肝脏酶促合成和水解。

  摘要：

  许多乙二醇衍生的溶剂被肝酶氧化为异种烷氧基乙酸（3-氧杂酸）。这些普遍存在的溶剂的毒性与其草酸代谢产物有关。对于许多异种生物羧酸而言，毒性与该酸的CoA酯有关。在这项研究中，相关的烷氧基乙酸被评估为在从大鼠肝脏分离的线粒体，过氧化物酶体和微粒体级分中发现的酰基辅酶A合成酶的潜在底物。同样，化学合成的氧杂酰基辅酶A被用作与相同大鼠肝部分相关的酰基辅酶A水解酶的底物。通过紫外可见分光光度法将异种生物被氧取代的底物的活性与类似的生理性脂肪族底物进行了比较。所有溶剂衍生的草酸都是酰基辅酶A合成酶的合理底物，尽管它们的活性通常低于相应的生理酸。与所有底物（特别是氧代酰基辅酶A）的酰基辅酶A合成酶活性相比，酰基辅酶A水解酶活性降低。这些研究表明，这些异源羧酸可被转化为反应性酰基辅酶A部分，这些部分将持续存在于脂质合成，β氧化，蛋白质酰化和氨基酸结合附近的细胞区域。这些异生物质酰基辅酶A与这些过程的相互

  DOI：

  10.1002/jbt.10063
• 作为产物：
  描述：

  正戊醛 、 辅酶 A 在 nonphosphorylating CoA-dependent aldehyde dehydrogenase from the polychlorinated biphenyl pollutant-degrading bacterium Burkholderia xenovorans LB₄₀₀ wild type 、 β-烟酰胺腺嘌呤二核苷酸 、 manganese(ll) chloride 作用下， 生成 pentanoyl coenzyme A
  参考文献：
  名称：

  Substrate Specificity, Substrate Channeling, and Allostery in BphJ: An Acylating Aldehyde Dehydrogenase Associated with the Pyruvate Aldolase BphI

  摘要：

  BphJ, a nonphosphorylating acylating aldehyde dehydrogenase, catalyzes the conversion of aldehydes to form acyl-coenzyme A in the presence of NAD(+) and coenzyme A (CoA). The enzyme is structurally related to the nonacylating aldehyde dehydrogenases, aspartate-β-semialdehyde dehydrogenase and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. Cys-131 was identified as the catalytic thiol in BphJ, and pH profiles together with site-specific mutagenesis data demonstrated that the catalytic thiol is not activated by an aspartate residue, as previously proposed. In contrast to the wild-type enzyme that had similar specificities for two- or three-carbon aldehydes, an I195A variant was observed to have a 20-fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate, acetaldehyde. BphJ forms a heterotetrameric complex with the class II aldolase BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel. Replacement of Ile-171 and Ile-195 with bulkier amino acid residues resulted in no more than a 35% reduction in acetaldehyde channeling efficiency, showing that these residues are not critical in gating the exit of the channel. Likewise, the replacement of Asn-170 in BphJ with alanine and aspartate did not substantially alter aldehyde channeling efficiencies. Levels of activation of BphI by BphJ N170A, N170D, and I171A were reduced by ≥3-fold in the presence of NADH and ≥4.5-fold when BphJ was undergoing turnover, indicating that allosteric activation of the aldolase has been compromised in these variants. The results demonstrate that the dehydrogenase coordinates the catalytic activity of BphI through allostery rather than through aldehyde channeling.

  DOI：

  10.1021/bi300407y

文献信息

• Repurposing the 3‐Isocyanobutanoic Acid Adenylation Enzyme SfaB for Versatile Amidation and Thioesterification
  作者：Mengyi Zhu、Lijuan Wang、Jing He

  DOI：10.1002/anie.202010042

  日期：2021.1.25

  molecules with novel skeletons, but also to identify the enzymes that catalyze diverse chemical reactions. Exploring the substrate promiscuity and catalytic mechanism of those biosynthetic enzymes facilitates the development of potential biocatalysts. SfaB is an acyl adenylate‐forming enzyme that adenylates a unique building block, 3‐isocyanobutanoic acid, in the biosynthetic pathway of the diisonitrile

  微生物天然产物的基因组挖掘使化学家不仅能够发现具有新颖骨架的生物活性分子，而且能够识别催化多种化学反应的酶。探索这些生物合成酶的底物混杂性和催化机理有助于开发潜在的生物催化剂。SfaB是一种形成酰基腺苷酸的酶，可在由硫链霉菌产生的二异腈自然产物SF2768的生物合成途径中，对独特的结构单元3-异氰基丁酸进行腺苷酸化。，并且该AMP连接酶被证明可以接受各种短链脂肪酸（SCFA）。在本文中，我们将SfaB重新用于催化那些SCFA与各种胺或硫醇亲核试剂之间的酰胺化或硫酯化反应，从而提供了另一种酶促方法来体外制备相应的酰胺和硫酯。
• [EN] A HOST CELL MODIFIED TO PRODUCE LACTAMS<br/>[FR] CELLULE HÔTE MODIFIÉE POUR PRODUIRE DES LACTAMES
  申请人：UNIV CALIFORNIA

  公开号：WO2017214159A1

  公开（公告）日：2017-12-14

  The present invention provides for a genetically modified host cell capable of producing a lactam comprising a 2-pyrrolidone synthase, or an enzymatically active fragment thereof, heterologous to the host cell.

  本发明提供了一种基因改造宿主细胞，能够产生一种内酰胺，其中包括一种对宿主细胞异源的2-吡咯烷酮合成酶或其酶活性片段。
• Screening and Engineering the Synthetic Potential of Carboxylating Reductases from Central Metabolism and Polyketide Biosynthesis
  作者：Dominik M. Peter、Lennart Schada von Borzyskowski、Patrick Kiefer、Philipp Christen、Julia A. Vorholt、Tobias J. Erb

  DOI：10.1002/anie.201505282

  日期：2015.11.2

  Carboxylating enoyl‐thioester reductases (ECRs) are a recently discovered class of enzymes. They catalyze the highly efficient addition of CO2 to the double bond of α,β‐unsaturated CoA‐thioesters and serve two biological functions. In primary metabolism of many bacteria they produce ethylmalonyl‐CoA during assimilation of the central metabolite acetyl‐CoA. In secondary metabolism they provide distinct

  羧化烯酰硫酯还原酶（ECR）是最近发现的一类酶。它们催化高效添加CO 2与α，β-不饱和CoA-硫酯的双键结合，具有两个生物学功能。在许多细菌的初级代谢中，它们在吸收中央代谢物乙酰辅酶A的过程中会产生乙基丙二酰辅酶A。在次级代谢中，它们提供独特的α-羧基-酰基-硫代酯，以改变许多聚酮化合物天然产物的主链。使用各种可能的底物库系统评估了不同的ECR。我们鉴定了三个活性位点残基，以区分仅限于C4和C5-烯酰基-CoA的ECR和高度混杂的ECR，并成功地设计了一种选定的ECR作为原理证明。这项研究定义了ECR反应性的分子基础，从而可以预测和操纵天然产物多样化中的关键反应。
• Identification of an α-Oxoamine Synthase and a One-Pot Two-Step Enzymatic Synthesis of α-Amino Ketones
  作者：Ting Zhou、Du Gao、Jia-Xin Li、Min-Juan Xu、Jun Xu

  DOI：10.1021/acs.orglett.0c03600

  日期：2021.1.1

  incorporation of l-glutamate to acyl-coenzyme A substrates. Combined with Alb29 and Mgr36 (an acyl-coenzyme A ligase), a one-pot enzymatic system was established to synthesize seven α-amino ketones. When these α-amino ketones were fed into the alb29 knockout strain Δalb29, respectively, the albogrisin analogs with different side chains were observed.

  Alb29 是一种 α-氧代胺合酶，参与Streptomyces albogriseolus MGR072中的 albogrisin 生物合成，被表征并负责将l-谷氨酸掺入酰基辅酶 A 底物。结合Alb29和Mgr36（一种酰基辅酶A连接酶），建立了一锅法合成七个α-氨基酮。当这些α-氨基酮分别加入alb29敲除菌株Δalb29时，观察到具有不同侧链的albogrisin类似物。
• ATP Regeneration System in Chemoenzymatic Amide Bond Formation with Thermophilic CoA Ligase
  作者：Chloé M. Lelièvre、Mélanie Balandras、Jean‐Louis Petit、Carine Vergne‐Vaxelaire、Anne Zaparucha

  DOI：10.1002/cctc.201901870

  日期：2020.2.20

  counterparts. To limit the use of ATP, we implemented an ATP regeneration system combining polyphosphate kinase 2 (PPK2 Class III) and inorganic pyrophosphatase. Suitability of this system was illustrated by the lab‐scale chemoenzymatic synthesis of N‐methylbutyrylamide in 77 % yield using low enzyme loading and 5 % molar ATP.

  CoA连接酶是通过腺苷酸中间体分两步催化ATP依赖的辅酶A加成到羧酸的酶。该中间体可通过亲核非酶加成胺而转移，以得到用于合成目的的相应酰胺。为此，我们选择了嗜热性CoA连接酶来研究各种羧酸向其酰胺对应物的转化。为了限制ATP的使用，我们实施了一个ATP再生系统，该系统结合了多磷酸激酶2（PPK2 III类）和无机焦磷酸酶。该系统的适用性通过实验室规模的化学酶法合成N-甲基丁酰酰胺，使用低酶负荷和5％摩尔ATP的产率为77％来说明。