methyl 5-stearamidopentanoate

• 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: methyl 5-stearamidopentanoate
• 英文别名: Methyl 5-(octadecanoylamino)pentanoate；methyl 5-(octadecanoylamino)pentanoate
• 化学式: C₂₄H₄₇NO₃
• 分子量: 397.642
• InChiKey: WIEOHFSRZXBELF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.5
• 重原子数：
  28
• 可旋转键数：
  22
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  methyl 5-stearamidopentanoate 在 lithium hydroxide 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 2.0h， 生成 5-stearamidopentanoic acid
  参考文献：
  名称：

  Biosynthesis of Long-Chain N-Acyl Amide by a Truncated Polyketide Synthase–Nonribosomal Peptide Synthetase Hybrid Megasynthase in Fungi

  摘要：

  Truncated iterative polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) megasynthases in which only the C domain is present are widespread in fungi, yet nearly all members have unknown functions. Bioinformatics analysis showed that the C domains of such PKS-C enzymes are noncanonical due to substitution at the second histidine in the active site HHxxxDG motif. Here, we used genome mining strategy to characterize a cryptic PKS-C hybrid from Talaromyces wortmanii and discovered the products are reduced long chain polyketides amidated with a specific omega-amino acid 5-aminopentanoic acid (5PA). The wortmanamides resemble long-chain N-acyl-amide signaling lipids that target diverse receptors including GPCRs. The noncanonical C domain of this PKS-C hybrid was also demonstrated to be a bona fide condensation domain that specifically selects 5PA and catalyzes amidation to release polyketide chain.

  DOI：

  10.1021/jacs.7b13350
• 作为产物：
  描述：

  5-氨基戊酸甲酯 、 硬脂酸 在 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 12.0h， 以68%的产率得到methyl 5-stearamidopentanoate
  参考文献：
  名称：

  Biosynthesis of Long-Chain N-Acyl Amide by a Truncated Polyketide Synthase–Nonribosomal Peptide Synthetase Hybrid Megasynthase in Fungi

  摘要：

  Truncated iterative polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) megasynthases in which only the C domain is present are widespread in fungi, yet nearly all members have unknown functions. Bioinformatics analysis showed that the C domains of such PKS-C enzymes are noncanonical due to substitution at the second histidine in the active site HHxxxDG motif. Here, we used genome mining strategy to characterize a cryptic PKS-C hybrid from Talaromyces wortmanii and discovered the products are reduced long chain polyketides amidated with a specific omega-amino acid 5-aminopentanoic acid (5PA). The wortmanamides resemble long-chain N-acyl-amide signaling lipids that target diverse receptors including GPCRs. The noncanonical C domain of this PKS-C hybrid was also demonstrated to be a bona fide condensation domain that specifically selects 5PA and catalyzes amidation to release polyketide chain.

  DOI：

  10.1021/jacs.7b13350

文献信息

• Biosynthesis of Long-Chain <i>N</i>-Acyl Amide by a Truncated Polyketide Synthase–Nonribosomal Peptide Synthetase Hybrid Megasynthase in Fungi
  作者：Yang Hai、Yi Tang

  DOI：10.1021/jacs.7b13350

  日期：2018.1.31

  Truncated iterative polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) megasynthases in which only the C domain is present are widespread in fungi, yet nearly all members have unknown functions. Bioinformatics analysis showed that the C domains of such PKS-C enzymes are noncanonical due to substitution at the second histidine in the active site HHxxxDG motif. Here, we used genome mining strategy to characterize a cryptic PKS-C hybrid from Talaromyces wortmanii and discovered the products are reduced long chain polyketides amidated with a specific omega-amino acid 5-aminopentanoic acid (5PA). The wortmanamides resemble long-chain N-acyl-amide signaling lipids that target diverse receptors including GPCRs. The noncanonical C domain of this PKS-C hybrid was also demonstrated to be a bona fide condensation domain that specifically selects 5PA and catalyzes amidation to release polyketide chain.