(E)-hept-2-enoate

• 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: (E)-hept-2-enoate
• 化学式: C7H11O2-
• 分子量: 127.16
• InChiKey: YURNCBVQZBJDAJ-AATRIKPKSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  40.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  (E)-2-庚烯醛 、 水 、 NADP⁺ 生成 (E)-hept-2-enoate 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  共表达分析确定了两个氧化还原酶参与了天然除虫菊酯杀虫剂单叶艾菊中单萜酸部分的生物合成。

  摘要：

  食草艾草的花产生了一组统称为除虫菊酯的化合物，这是商业上重要的农药，对飞行的昆虫有强烈的毒性，但对大多数脊椎动物没有毒性。拟除虫菊酯分子是一种酯，它由反菊糖酸或其修饰形式，除虫菊酸和三种醇（茉莉酮，除虫菊酯和肉桂酮）中的一种组成，它们似乎是从茉莉酸衍生而来的。菊酯二磷酸合酶（CDS）是第一个参与反菊酸合成的酶，此前已进行了表征并分离了其基因。TcCDS除反式菊二磷酸酯外还产生游离的反式菊糖，但尚未报道负责将反式菊糖转化为相应的醛然后转化为酸的酶。我们使用基于RNA测序的方法和共表达相关性分析来鉴定编码推定的反式菊花和反式菊花脱氢酶的几种候选基因。我们使用体外生化分析和植物中的异源表达相结合的方法，对这些基因编码的蛋白质进行了功能鉴定，以证明TcADH2编码一种将反式菊花转化为反式菊花的酶，而TcALDH1编码的一种将氧化式菊花转化成的酶。反式菊苣酸。TcADH2和TcALDH1与TcCDS

  DOI：

  10.1104/pp.17.01330

文献信息

• Molecular Cloning and Oxidative Modification of Human Lens ALDH1A1: Implication in Impaired Detoxification of Lipid Aldehydes
  作者：Tianlin Xiao、Mohammad Shoeb、M. Saeed Siddiqui、Min Zhang、Kota V. Ramana、Satish K. Srivastava、Vasilis Vasiliou、Naseem H. Ansari

  DOI：10.1080/15287390802706371

  日期：2009.3.27

  Earlier studies showed that human lens ALDH1A1 plays a critical role in protection against oxidative stress-induced cytotoxicity in human lens epithelial cells (HLEC), and opacification of rat and mouse lens. The complete coding sequence of ALDH1A1 was cloned from human lens cDNA library by using PCR methods and expressed it in Escherichia coli. The cloned human lens ALDH1A1 cDNA encodes a 501-amino-acid protein (molecular mass = 54.8 kD) that is 100% identical to human liver ALDH1A1 and shares significant identity with the same isozyme from other tissues and species. The purified recombinant human lens ALDH1A1 exhibited optimal catalytic activity at pH 8 and preferred NAD+ as cofactor and specifically catalyzed the oxidation of toxic lipid aldehydes such as 4-hydroxynonenal (HNE; Km = 4.8 M) and malonaldehyde (Km MDA = 3.5 M). Citral, disulfiram, and cyanamide were found to inhibit human lens ALDH1A1 at IC50 values of 55, 101, and 22610 M, respectively, whereas diethylstilbestrol (DES) was found to be an activator (EC50, 1.3 M). Further, modification of recombinant human lens ALDH1A1 with nitric oxide donors such as S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO) significantly inhibited the enzyme activity. It therefore appears that activation of ALDH1A1, which efficiently catalyzes the detoxification of lipid-derived toxic aldehydes, and/or prevention of its oxidative modification may be novel therapeutic interventions against oxidative stress-induced lens pathologies.