ricinoleoyl-CoA

• 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: ricinoleoyl-CoA
• 英文别名: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[[[(3R)-3-hydroxy-4-[[3-[2-[(Z,12R)-12-hydroxyoctadec-9-enoyl]sulfanylethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutoxy]-oxidophosphoryl]oxy-oxidophosphoryl]oxymethyl]oxolan-3-yl] phosphate
• 化学式: C39H64N7O18P3S-4
• 分子量: 1043.9
• InChiKey: BHVZCCKRRPYXCV-MGNVXPIMSA-J

计算性质

• 辛醇/水分配系数(LogP)：
  0
• 重原子数：
  68
• 可旋转键数：
  34
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.74
• 拓扑面积：
  421
• 氢给体数：
  6
• 氢受体数：
  23

反应信息

• 作为反应物：
  描述：

  ricinoleoyl-CoA 、 甘磷酸胆碱 生成 (12R-hydroxy-9Z-octadecenoyl)-sn-glycero-3-phosphocholine 、 coenzyme A
  参考文献：
  名称：

  从真菌和植物克隆甘油磷酸胆碱酰基转移酶（GPCAT）：磷脂酰胆碱合成中的新型酶。

  摘要：

  长期以来一直认为磷脂酰胆碱（PC）完全脱酰的产物甘油3-磷酸胆碱（GPC）并不是再酰化的底物。然而，最近显示，来自酵母和植物的无细胞提取物可将GPC与来自酰基辅酶A的酰基酰化。通过筛选来自酵母敲除集合的提取物的酶活性，我们能够鉴定和克隆编码该酶的酵母基因（GPC1），称为甘油磷酸胆碱酰基转移酶（GPCAT）。通过同源搜索，我们还从三种植物中鉴定并克隆了GPCAT基因。所有酶都利用酰基辅酶A酰化GPC，形成溶血PC，并且它们在酵母和植物中均显示出广泛的酰基特异性。除酰基辅酶A外，GPCAT还有效地利用LPC和溶血磷脂酰乙醇胺作为酰基化GPC的酰基供体。在主要的真核生物组中发现了GPCAT同源物，但在原核生物或脊索动物中未发现GPCAT同源物。该酶形成自己的蛋白质家族，不包含其他研究过的酰基转移酶和转酰酶中存在的任何酰基结合或脂肪酶基序。体内标记研究证实了Gpc1p在酵母PC生物合成中的作用。

  DOI：

  10.1074/jbc.m116.743062

文献信息

• Identification and functional expression of a type 2 acyl-CoA:diacylglycerol acyltransferase (DGAT2) in developing castor bean seeds which has high homology to the major triglyceride biosynthetic enzyme of fungi and animals
  作者：Johan T.M. Kroon、Wenxue Wei、William J. Simon、Antoni R. Slabas

  DOI：10.1016/j.phytochem.2006.09.020

  日期：2006.12

  Seed oil from castor bean (Ricinus communis) contains high amounts of hydroxy fatty acid rich triacyl glycerols (TAGs) that can serve as raw material for production of bio-based products such as nylon, cosmetics, lubricants, foams, and surfactants. Diacylglycerol acyltransferase (DGAT) catalyses the terminal reaction in the acyl-CoA dependent Kennedy pathway of triglyceride biosynthesis. There is still some debate whether there are three or four enzymes in yeast that have DGAT activity and catalyse the synthesis of TAG but of these the DGAT2 homologue Dga1 contributes in a major way to TAG biosynthesis. Here we report on the cloning of a cDNA for DGAT2 from castor bean and prove its biological activity following expression in yeast and enzymatic assays using diricinolein as the acceptor and ricinoleoyl-CoA as the donor. Previous reports of DGAT in castor have focussed on DGAT1 which has little amino acid sequence homology to DGAT2. Expressional studies demonstrate that DGAT2 is 18-fold more highly expressed in seeds than in leaves and shows temporal specific expression during seed development. In contrast, DGAT1 shows little difference in expression in seeds versus leaves. We conclude that in castor bean DGAT2 is more likely to play a major role in seed TAG biosynthesis than DGAT1. (c) 2006 Elsevier Ltd. All rights reserved.
• Cloning of Glycerophosphocholine Acyltransferase (GPCAT) from Fungi and Plants
  作者：Bartosz Głąb、Mirela Beganovic、Sanket Anaokar、Meng-Shu Hao、Allan G. Rasmusson、Jana Patton-Vogt、Antoni Banaś、Sten Stymne、Ida Lager

  DOI：10.1074/jbc.m116.743062

  日期：2016.11

  extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize

  长期以来一直认为磷脂酰胆碱（PC）完全脱酰的产物甘油3-磷酸胆碱（GPC）并不是再酰化的底物。然而，最近显示，来自酵母和植物的无细胞提取物可将GPC与来自酰基辅酶A的酰基酰化。通过筛选来自酵母敲除集合的提取物的酶活性，我们能够鉴定和克隆编码该酶的酵母基因（GPC1），称为甘油磷酸胆碱酰基转移酶（GPCAT）。通过同源搜索，我们还从三种植物中鉴定并克隆了GPCAT基因。所有酶都利用酰基辅酶A酰化GPC，形成溶血PC，并且它们在酵母和植物中均显示出广泛的酰基特异性。除酰基辅酶A外，GPCAT还有效地利用LPC和溶血磷脂酰乙醇胺作为酰基化GPC的酰基供体。在主要的真核生物组中发现了GPCAT同源物，但在原核生物或脊索动物中未发现GPCAT同源物。该酶形成自己的蛋白质家族，不包含其他研究过的酰基转移酶和转酰酶中存在的任何酰基结合或脂肪酶基序。体内标记研究证实了Gpc1p在酵母PC生物合成中的作用。