2-(Hexadecanoylamino)acetate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-(Hexadecanoylamino)acetate
• 化学式: C18H34NO3-
• 分子量: 312.5
• InChiKey: KVTFEOAKFFQCCX-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  7.1
• 重原子数：
  22
• 可旋转键数：
  15
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  69.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  聚甘氨酸 、 hexadecanoyl CoA 生成 coenzyme A 、 氢(+1)阳离子 、 2-(Hexadecanoylamino)acetate
  参考文献：
  名称：

  甘氨酸N-酰基转移酶样3负责N18TG2细胞中长链N-酰基甘氨酸的形成。

  摘要：

  长链脂肪酸酰胺是在哺乳动物和其他生物中发现的脂质信号。然而，关于N-酰基甘氨酸和伯脂肪酸酰胺（PFAM）的代谢途径的细节仍然难以捉摸。小鼠神经母细胞瘤N18TG2细胞（用于研究脂肪酸酰胺代谢的模型细胞系）中的重标记前体和减体脂质组学实验建立了N-酰基甘氨酸和PFAM的生物合成途径。我们提供的证据表明，N-酰基甘氨酸是由长链特异性甘氨酸缀合酶甘氨酸N-酰基转移酶样3（GLYATL3）形成的。N18TG2细胞中GLYATL3的siRNA敲低导致N-酰基甘氨酸和PFAM的水平降低。这是有关纤维素中长链N-酰基甘氨酸生产的酶的首次报道。据报道，N18TG2细胞中PFAM的产生是由于N-酰基甘氨酸的氧化裂解，如肽基甘氨酸α-酰胺化单加氧酶（PAM）的催化。当N18TG2细胞在[（13）C18]油酸存在下生长时，PAM的siRNA敲低导致[（13）C18] N-油酰甘氨酸的积累和[（13）C18]油酰

  DOI：

  10.1194/jlr.m062042

文献信息

• Identification of glycine<i>N</i>‐acyltransferase‐like 2 (GLYATL2) as a transferase that produces<i>N</i>‐acyl glycines in humans
  作者：Dominik P. Waluk、Niklas Schultz、Mary C. Hunt

  DOI：10.1096/fj.09-148551

  日期：2010.8

  The discovery of glycine conjugates of long-chain fatty acids (N-acyl glycines) in the brain and other non-neuronal tissues has led to the identification of an emerging class of bioactive lipids. The biological activities of N-acyl glycines include antinociceptive, anti-inflammatory and antiproliferative effects, and activation of G-protein-coupled receptors. However, despite the fact that N-acyl glycines are emerging as a distinct lipid signaling family, pathways for their production are not fully elucidated. Here we report on the characterization of human glycine N-acyltransferase-like 2 (hGLYATL2), a member of a gene family of 4 putative glycine conjugating enzymes, and show that it synthesizes various N-acyl glycines. Recombinantly expressed hGLYATL2 efficiently conjugated oleoyl-CoA, arachidonoyl-CoA, and other medium-and long-chain acyl-CoAs to glycine. The enzyme was specific for glycine as an acceptor molecule, and preferentially produced N-oleoyl glycine. The hGLYATL2 enzyme is localized to the endoplasmic reticulum, and the mRNA shows highest expression in salivary gland and trachea, but is also detected in spinal cord and skin fibroblasts. The expression pattern and the identification of high levels of N-acyl glycines in skin and lung may indicate a role for N-acyl glycines in barrier function/immune response and the potential role of hGLYATL2 in this regard is discussed.-Waluk, D. P., Schultz, N., Hunt, M. C. Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a transferase that produces N-acyl glycines in humans. FASEB J. 24, 2795-2803 (2010). www.fasebj.org