4-Hydroxy-6-(2-oxoheptadecyl)pyran-2-one | 889131-95-7

• 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-oxoheptadecyl)pyran-2-one
• 英文别名: 4-hydroxy-6-(2-oxoheptadecyl)pyran-2-one
• CAS: 889131-95-7
• 化学式: C₂₂H₃₆O₄
• 分子量: 364.525
• InChiKey: PWJCIKPTDVJSCJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.1
• 重原子数：
  26
• 可旋转键数：
  16
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.73
• 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 、 棕榈酰辅酶A,钾盐 在 Botrytis cinerea type III polyketide synthase 作用下， 生成 4-Hydroxy-6-(2-oxoheptadecyl)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。
• 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。
• 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.
• The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs
  作者：Marimuthu Jeya、Tae-Su Kim、Manish Kumar Tiwari、Jinglin Li、Huimin Zhao、Jung-Kul Lee

  DOI：10.1039/c2mb25282a

  日期：——

  BPKS from Botrytis cinerea is a novel type III polyketide synthase that accepts C4–C18 aliphatic acyl-CoAs and benzoyl-CoA as the starters to form pyrones, resorcylic acids and resorcinols through sequential condensation with malonyl-CoA. The catalytic efficiency (kcat/Km) of BPKS was 2.8 × 105 s−1 M−1 for palmitoyl-CoA, the highest ever reported. Substrate docking analyses addressed the unique features of BPKS such as its high activity and high specificity toward long chain acyl-CoAs.

  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。