4-Hydroxy-6-(2-oxononadecyl)pyran-2-one | 889131-94-6

• 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-oxononadecyl)pyran-2-one
• 英文别名: 4-hydroxy-6-(2-oxononadecyl)pyran-2-one
• CAS: 889131-94-6
• 化学式: C₂₄H₄₀O₄
• 分子量: 392.579
• InChiKey: GBAFNXLIBBSENQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.2
• 重原子数：
  28
• 可旋转键数：
  18
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.75
• 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 、 硬脂酰辅酶A 在 Botrytis cinerea type III polyketide synthase 作用下， 生成 4-Hydroxy-6-(2-oxononadecyl)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

• A type III polyketide synthase from Rhizobium etli condenses malonyl CoAs to a heptaketide pyrone with unusually high catalytic efficiency
  作者：Marimuthu Jeya、Tae-Su Kim、Manish Kumar Tiwari、Jinglin Li、Huimin Zhao、Jung-Kul Lee

  DOI：10.1039/c2mb25347j

  日期：——

  A novel type III polyketide synthase (RePKS) from Rhizobium etli produced a heptaketide pyrone using acetyl-CoA and six molecules of malonyl-CoA. Its catalytic efficiency (kcat/Km = 5230 mM−1 min−1) for malonyl CoA was found to be the highest ever reported. Molecular dynamics studies revealed the unique features of RePKS.

  一种来自根瘤菌（Rhizobium etli）的新型 III 型多酮合成酶（RePKS）利用乙酰-CoA 和六分子丙二酰-CoA 生成了一种七酮吡咯烷酮。它对丙二酰 CoA 的催化效率（kcat/Km = 5230 mM-1 min-1）是迄今所报道的最高的。分子动力学研究揭示了 RePKS 的独特之处。
• 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.
• A New Family of Type III Polyketide Synthases in Mycobacterium tuberculosis
  作者：Priti Saxena、Gitanjali Yadav、Debasisa Mohanty、Rajesh S. Gokhale

  DOI：10.1074/jbc.m306714200

  日期：2003.11

  The Mycobacterium tuberculosis genome has revealed a remarkable array of polyketide synthases (PKSs); however, no polyketide product has been isolated thus far. Most of the PKS genes have been implicated in the biosynthesis of complex lipids. We report here the characterization of two novel type III PKSs from M. tuberculosis that are involved in the biosynthesis of long-chain alpha-pyrones. Measurement of steady-state kinetic parameters demonstrated that the catalytic efficiency of PKS18 protein was severalfold higher for long-chain acyl-coenzyme A substrates as compared with the small-chain precursors. The specificity of PKS18 and PKS11 proteins toward long-chain aliphatic acyl-coenzyme A (C-12 to C-20) substrates is unprecedented in the chalcone synthase (CHS) family of condensing enzymes. Based on comparative modeling studies, we propose that these proteins might have evolved by fusing the catalytic machinery of CHS and beta-ketoacyl synthases, the two evolutionarily related members with conserved thiolase fold. The mechanistic and structural importance of several active site residues, as predicted by our structural model, was investigated by performing site-directed mutagenesis. The functional identification of diverse catalytic activity in mycobacterial type III PKSs provide a fascinating example of metabolite divergence in CHS-like proteins.