4-hydroxy-6-(2-oxotridecyl)pyran-2-one | 640279-93-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡喃
• 英文名称: 4-hydroxy-6-(2-oxotridecyl)pyran-2-one
• 英文别名: 4-Hydroxy-6-(2-oxotridecyl)pyran-2-one
• CAS: 640279-93-2
• 化学式: C₁₈H₂₈O₄
• 分子量: 308.418
• InChiKey: GPSLPPYNZMBYDU-UHFFFAOYSA-N

物化性质

• 沸点：
  440.5±45.0 °C(Predicted)
• 密度：
  1.064±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.9
• 重原子数：
  22
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  63.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  丙二酰辅酶A-钠盐 、 辅酶 A-S-月桂酸酯 在 Botrytis cinerea type III polyketide synthase 作用下， 生成 4-hydroxy-6-(2-oxotridecyl)pyran-2-one
  参考文献：
  名称：

  The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs

  摘要：

  葡萄孢菌（Botrytis cinerea）中的BPKS是一种新型III型聚酮合酶，能够接受C4-C18的脂肪酰辅酶A和苯甲酰辅酶A作为起始物，通过与丙二酰辅酶A的连续缩合反应形成吡喃酮、间苯二酚酸和间苯二酚。BPKS对棕榈酰辅酶A的催化效率（kcat/Km）高达2.8 × 10^5 s^-1 M^-1，是有史以来报道的最高值。底物对接分析揭示了BPKS独特的特性，如其对长链酰基辅酶A的高活性和高特异性。

  DOI：

  10.1039/c2mb25282a

文献信息

• Exploiting the Reaction Flexibility of a Type III Polyketide Synthase through in Vitro Pathway Manipulation
  作者：Jae-Cheol Jeong、Aravind Srinivasan、Sabine Grüschow、Horacio Bach、David H. Sherman、Jonathan S. Dordick

  DOI：10.1021/ja0441559

  日期：2005.1.1

  synthesis of the pentaketide flaviolin and its dimeric derivative, and a wide range of pyrones and their coupled derivatives with flaviolin, as well as their halogenated derivatives. The addition of acyl-CoA oxidase to the pathway prior to the polyketide synthase resulted in unsaturated pyrone side chains, further broadening the product spectrum that can be achieved. The approach developed in this work

  在体外构建了一个合成代谢途径，包括来自天蓝色链霉菌的 III 型聚酮化合物合酶和来自大豆和烟熏蓝藻（氯过氧化物酶）的过氧化物酶。这导致合成了五肽黄素及其二聚衍生物，以及广泛的吡喃酮及其与黄素的偶联衍生物，以及它们的卤化衍生物。在聚酮合酶之前将酰基辅酶A氧化酶添加到途径中导致不饱和的吡喃酮侧链，进一步拓宽了可以实现的产物谱。因此，这项工作中开发的方法为在复杂天然产物衍生物的合成中利用生物催化提供了一种新模型。
• Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases
  作者：Ikuro Abe、Tatsuya Watanabe、Hiroshi Noguchi

  DOI：10.1016/j.phytochem.2004.08.005

  日期：2004.9

  synthase (CHS) from Scutellaria baicalensis and stilbene synthase (STS) from Arachis hypogaea accepted CoA esters of long-chain fatty acid (CHS up to the C12 ester, while STS up to the C14 ester) as a starter substrate, and carried out sequential condensations with malonyl-CoA, leading to formation of triketide and tetraketide alpha-pyrones. Interestingly, the C6, C8, and C10 esters were kinetically

  黄芩的重组查耳酮合酶 (CHS) 和花生的二苯乙烯合酶 (STS) 接受长链脂肪酸的 CoA 酯（CHS 到 C12 酯，而 STS 到 C14 酯）作为起始底物，并携带与丙二酰辅酶A连续缩合，导致三酮和四酮α-吡喃酮的形成。有趣的是，与生理起始底物相比，C6、C8 和 C10 酯在动力学上更受酶的青睐。kcat/KM 值比对香豆酰辅酶 A 高 1.2 至 1.9 倍。这些酶的催化多样性为 III 型 PKS 反应提供了进一步的机理见解，并表明 CHS 超家族酶参与了植物中长链烷基多酚（如漆酚和银杏酸）的生物合成。
• A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites
  作者：Rajan Sankaranarayanan、Priti Saxena、Uttara B Marathe、Rajesh S Gokhale、Vellaiah M Shanmugam、Raju Rukmini

  DOI：10.1038/nsmb809

  日期：2004.9

  The superfamily of plant and bacterial type III polyketide synthases (PKSs) produces diverse metabolites with distinct biological functions. PKS18, a type III PKS from Mycobacterium tuberculosis, displays an unusual broad specificity for aliphatic long-chain acyl-coenzyme A (acyl-CoA) starter units (C(6)-C(20)) to produce tri- and tetraketide pyrones. The crystal structure of PKS18 reveals a 20 A substrate

  植物和细菌III型聚酮化合物合酶（PKS）的超家族产生具有独特生物学功能的多种代谢产物。PKS18，来自结核分枝杆菌的III型PKS，对脂族长链酰基辅酶A（酰基-CoA）起始单元（C（6）-C（20））显示出异常的广泛特异性，可产生三酮和四酮化合物的吡喃酮。PKS18的晶体结构揭示了20 A的底物结合通道，迄今为止在该酶超家族中尚未发现。这种引人注目的隧道从蛋白质的活性位点延伸到蛋白质的表面，并且主要是由蛋白质核心中主链二面角的细微变化产生的。诱变研究与结构确定相结合，提供了对有助于酶链长特异性的结构元件的分子洞察力。
• Alkylresorcylic acid synthesis by type III polyketide synthases from rice Oryza sativa
  作者：Miku Matsuzawa、Yohei Katsuyama、Nobutaka Funa、Sueharu Horinouchi

  DOI：10.1016/j.phytochem.2010.02.012

  日期：2010.7

  Alkylresorcinols, produced by various plants, bacteria, and fungi, are bioactive compounds possessing beneficial activities for human health, such as anti-cancer activity. In rice, they accumulate in seedlings, contributing to protection against fungi. Alkylresorcylic acids, which are carboxylated forms of alkylresorcinols, are unstable compounds and decarboxylate readily to yield alkylresorcinols. Genome mining of the rice Oryza sativa identified two type III polyketide synthases, named ARAS1 (alkylresorcylic acid synthase) and ARAS2, that catalyze the formation of alkylresorcylic acids. Both enzymes condensed fatty acyl-CoAs with three C-2 units from malonyl-CoA and cyclized the resulting tetraketide intermediates via intramolecular C-2 to C-7 aldol condensation. The alkylresorcylic acids thus produced were released from the enzyme and decarboxylated non-enzymatically to yield alkylresorcinols. This is the first report on a plant type III polyketide synthase that produces tetraketide alkylresorcylic acids as major products. (C)2010 Published by Elsevier Ltd.
• Promiscuous Fatty Acyl CoA Ligases Produce Acyl-CoA and Acyl-SNAC Precursors for Polyketide Biosynthesis
  作者：Pooja Arora、Archana Vats、Priti Saxena、Debasisa Mohanty、Rajesh S. Gokhale

  DOI：10.1021/ja052991s

  日期：2005.7.1

  The study of bioactive natural products has undergone rapid advancement with the cloning and sequencing of large number of gene clusters and the concurrent progress to manipulate complex biosynthetic systems in heterologous hosts. The genetic reconstitution necessitates that the heterologous hosts possess substrate pools that could be coordinately supplied for biosynthesis. Polyketide synthases (PKS) utilize acyl-coenzyme A (CoA) precursors and synthesize polyketides by repetitive decarboxylative condensations. Here we show that acyl-CoA ligases, which belong to a large family of acyl-activating enzymes, possess potential to produce varied starter CoA precursors that could be utilized in polyketide biosynthesis. Incidentally, such protein domains have been recognized in several PKS and nonribosomal peptide synthetase gene clusters. Our studies with mycobacterial fatty acyl-CoA ligases (FACLs) show remarkable tolerance to activate a variety of fatty acids that contain modifications at alpha, beta, omega, and omega-nu positions. This substrate flexibility extends further such that these proteins also efficiently utilize N-acetyl cysteamine, the shorter acceptor terminal portion of CoASH, to produce acyl-SNACs. We show that the in situ generated acyl-CoAs and acyl-SNACs could be channeled to types I and -III PKS systems to produce new metabolites. Together, the promiscuous activity of FACL and PKSs provides new opportunities to expand the repertoire of natural products.