(9Z,12Z)-18-hydroxyoctadecadienoyl-CoA(4-)

• 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: (9Z,12Z)-18-hydroxyoctadecadienoyl-CoA(4-)
• 英文别名: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[[[(3R)-3-hydroxy-4-[[3-[2-[(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoyl]sulfanylethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutoxy]-oxidophosphoryl]oxy-oxidophosphoryl]oxymethyl]oxolan-3-yl] phosphate
• 化学式: C39H62N7O18P3S-4
• 分子量: 1041.9
• InChiKey: HJEGYLSHIKPENR-DAXVLCLXSA-J

计算性质

• 辛醇/水分配系数(LogP)：
  -0.8
• 重原子数：
  68
• 可旋转键数：
  34
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  421
• 氢给体数：
  6
• 氢受体数：
  23

反应信息

• 作为产物：
  描述：

  linoleoyl-CoA(4-) 、 氧气 、 1-Deoxy-1-(7,8-dimethyl-2,4-dioxidobenzo[g]pteridin-10(5H)-yl)-5-O-phosphonopentitol 生成 (9Z,12Z)-18-hydroxyoctadecadienoyl-CoA(4-) 、 氢(+1)阳离子 、 水 、 FMN
  参考文献：
  名称：

  Expression and Characterization of CYP52 Genes Involved in the Biosynthesis of Sophorolipid and Alkane Metabolism from Starmerella bombicola

  摘要：

  摘要 三种细胞色素 P450 单加氧酶 CYP52 基因家族成员从产槐脂酵母 酵母 前 念珠菌 )中分离出CYP52基因家族成员，即 CYP52E3 , CYP52M1 和 CYP52N1 及其开放阅读框克隆到 pYES2 载体中，以便在 酵母中表达。 .使用微粒体蛋白或全细胞系统分析了重组蛋白在多种烷烃和脂肪酸底物中的功能。研究发现 CYP52M1 可氧化 C 16 氧化为 C 20 脂肪酸。它将油酸（C 18:1 ）比硬脂酸（C 18:0 ）和亚油酸（C 18:2 比硬脂酸（C 18:0 ）和亚油酸（C 18:2 ）更有效，比 α-亚麻酸（C 18:3 ).当 C 10 至 C 12 脂肪酸作为底物时，未检测到产物。此外，CYP52M1 对脂肪酸的 ω- 和 ω-1 位进行羟化。CYP52N1 氧化 C 14 氧化为 C 20 饱和及不饱和脂肪酸，并优先氧化棕榈酸、油酸和亚油酸。它只催化脂肪酸的ω-羟基化。CYP52E3 对肉豆蔻酸、棕榈酸、棕榈油酸和油酸的ω-羟化活性较小。此外，还对这三种 P450 与葡萄糖基转移酶 UGTA1 进行了共同测定。UGTA1 对 CYP52E3、CYP52M1 和 CYP52N1 产生的所有羟基脂肪酸进行糖基化。CYP52M1/UGTA1 将脂肪酸转化为糖脂的效率远远高于 CYP52N1/UGTA1 和 CYP52E3/UGTA1。综上所述，CYP52M1 被证明参与了槐脂的生物合成，而 CYP52E3 和 CYP52N1 则可能参与了烷烃的代谢。 S. bombicola 但处于初始氧化步骤的下游。

  DOI：

  10.1128/aem.02886-13

文献信息

• The Cytochrome P450 CYP86A22 Is a Fatty Acyl-CoA ω-Hydroxylase Essential for Estolide Synthesis in the Stigma of Petunia hybrida
  作者：Jixiang Han、Joel M. Clement、Jia Li、Andrew King、Shirley Ng、Jan G. Jaworski

  DOI：10.1074/jbc.m109.050765

  日期：2010.2

  The stigmatic estolide is a lipid-based polyester constituting the major component of exudate in solanaceous plants. Although the exudate is believed to play important roles in the pollination process, the biosynthetic pathway of stigmatic estolide, including genes encoding the key enzymes, remains unknown. Here we report the cloning and characterization of the cytochrome P450 gene CYP86A22, which encodes a fatty acyl-CoA omega-hydroxylase involved in estolide biosynthesis in the stigma of Petunia hybrida. A CYP86A22 cDNA was isolated from a developing stigma cDNA library, and the corresponding gene was shown to express predominantly in the developing stigma. Among six P450 genes isolated from this library, only CYP86A22 was implicated in omega-hydroxylation following RNA interference (RNAi)-mediated suppression. Unlike wild-type plants in which omega-hydroxy fatty acids (mainly in the form of 18-hydroxy oleic acid and 18-hydroxy linoleic acid) compose 96% of total stigma fatty acids, the omega-hydroxy fatty acids were essentially absent in the stigmas from 18 of 46 CYP86A22-RNAi transgenic plants and had varying levels of suppression in the remaining 28 plants. Furthermore, lipids in the 18 CYP86A22-RNAi stigmas were predominantly triacylglycerols and diacylglycerols instead of the estolides, which characterize the wild-type stigma. Analyses of recombinant CYP86A22 conclusively demonstrated that this P450 is a omega-hydroxylase with a substrate preference for both saturated and unsaturated acyl-CoAs rather than free fatty acids. We conclude that the cytochrome P450 enzyme CYP86A22 is the key fatty acyl-CoA omega-hydroxylase essential for the production of omega-hydroxy fatty acids and the biosynthesis of triacylglycerol-/diacylglycerol-based estolide polyesters in the petunia stigma.
• Expression and Characterization of <i>CYP52</i> Genes Involved in the Biosynthesis of Sophorolipid and Alkane Metabolism from Starmerella bombicola
  作者：Fong-Chin Huang、Alyssa Peter、Wilfried Schwab

  DOI：10.1128/aem.02886-13

  日期：2014.1.15

  Three cytochrome P450 monooxygenase CYP52 gene family members were isolated from the sophorolipid-producing yeast Starmerella bombicola (former Candida bombicola ), namely, CYP52E3 , CYP52M1 , and CYP52N1 , and their open reading frames were cloned into the pYES2 vector for expression in Saccharomyces cerevisiae . The functions of the recombinant proteins were analyzed with a variety of alkane and fatty acid substrates using microsome proteins or a whole-cell system. CYP52M1 was found to oxidize C ₁₆ to C ₂₀ fatty acids preferentially. It converted oleic acid (C _18:1 ) more efficiently than stearic acid (C _18:0 ) and linoleic acid (C _18:2 ) and much more effectively than α-linolenic acid (C _18:3 ). No products were detected when C ₁₀ to C ₁₂ fatty acids were used as the substrates. Moreover, CYP52M1 hydroxylated fatty acids at their ω- and ω-1 positions. CYP52N1 oxidized C ₁₄ to C ₂₀ saturated and unsaturated fatty acids and preferentially oxidized palmitic acid, oleic acid, and linoleic acid. It only catalyzed ω-hydroxylation of fatty acids. Minor ω-hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid was shown for CYP52E3. Furthermore, the three P450s were coassayed with glucosyltransferase UGTA1. UGTA1 glycosylated all hydroxyl fatty acids generated by CYP52E3, CYP52M1, and CYP52N1. The transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 was much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1. Taken together, CYP52M1 is demonstrated to be involved in the biosynthesis of sophorolipid, whereas CYP52E3 and CYP52N1 might be involved in alkane metabolism in S. bombicola but downstream of the initial oxidation steps.

  摘要 三种细胞色素 P450 单加氧酶 CYP52 基因家族成员从产槐脂酵母 酵母 前 念珠菌 )中分离出CYP52基因家族成员，即 CYP52E3 , CYP52M1 和 CYP52N1 及其开放阅读框克隆到 pYES2 载体中，以便在 酵母中表达。 .使用微粒体蛋白或全细胞系统分析了重组蛋白在多种烷烃和脂肪酸底物中的功能。研究发现 CYP52M1 可氧化 C 16 氧化为 C 20 脂肪酸。它将油酸（C 18:1 ）比硬脂酸（C 18:0 ）和亚油酸（C 18:2 比硬脂酸（C 18:0 ）和亚油酸（C 18:2 ）更有效，比 α-亚麻酸（C 18:3 ).当 C 10 至 C 12 脂肪酸作为底物时，未检测到产物。此外，CYP52M1 对脂肪酸的 ω- 和 ω-1 位进行羟化。CYP52N1 氧化 C 14 氧化为 C 20 饱和及不饱和脂肪酸，并优先氧化棕榈酸、油酸和亚油酸。它只催化脂肪酸的ω-羟基化。CYP52E3 对肉豆蔻酸、棕榈酸、棕榈油酸和油酸的ω-羟化活性较小。此外，还对这三种 P450 与葡萄糖基转移酶 UGTA1 进行了共同测定。UGTA1 对 CYP52E3、CYP52M1 和 CYP52N1 产生的所有羟基脂肪酸进行糖基化。CYP52M1/UGTA1 将脂肪酸转化为糖脂的效率远远高于 CYP52N1/UGTA1 和 CYP52E3/UGTA1。综上所述，CYP52M1 被证明参与了槐脂的生物合成，而 CYP52E3 和 CYP52N1 则可能参与了烷烃的代谢。 S. bombicola 但处于初始氧化步骤的下游。