(2R)-2-乙酰氨基-3-[(Z)-1,2-二氯乙烯基]硫基丙酸 | 2148-31-4

• 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
• 中文名称: (2R)-2-乙酰氨基-3-[(Z)-1,2-二氯乙烯基]硫基丙酸
• 英文名称: N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
• 英文别名: S-(1,2-dichlorovinyl)-N-acetyl-L-cysteine；(2R)-2-Acetamido-3-(1,2-dichloroethenylsulfanyl)propanoic acid
• CAS: 2148-31-4
• 化学式: C₇H₉Cl₂NO₃S
• 分子量: 258.125
• InChiKey: LPPJGTSPIBSYQO-YFKPBYRVSA-N

物化性质

• 熔点：
  101-103°C
• 溶解度：
  可溶于乙腈（少许）、DMSO（少许）、甲醇（少许）

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  14
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  91.7
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 海关编码：
  2930909090

反应信息

• 作为反应物：
  描述：

  (2R)-2-乙酰氨基-3-[(Z)-1,2-二氯乙烯基]硫基丙酸 在 rat kidney acylase 作用下， 以 phosphate buffer 为溶剂， 反应 0.5h， 生成 S-(1,2-二氯乙烯基)半胱氨酸
  参考文献：
  名称：

  Acylase-Catalyzed Deacetylation of Haloalkene-Derived Mercapturates

  摘要：

  Mercapturates (S-substituted N-acetyl-L-cysteines) are terminal metabolites formed by the glutathione-dependent metabolism of electrophilic xenobiotics, including haloalkenes. Acylases catalyze the hydrolysis of N-acyl-L-amino acids, including many xenobiotic-derived mercapturates, to give fatty acids and amino acids as products. Although several acylases have been identified, the acylases that catalyze the deacetylation of the haloalkene-derived mercapturates have not been identified and characterized. Acylase I catalyzes the deacetylation of some haloalkene-derived mercapturates, including S-(1,1,2,2-tetrafluoroethyl)-N-acetyl-L-cysteine, S-(2-chloro-1,1,2-trifluoroethyl)-N-acetyl-cysteine, and S-(2-bromo-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine [Uttamsingh, V., et al. (1998) Chem. Res. Toxicol. 11, 800-809]. In the studies presented here, we identified a rat kidney acylase that catalyzed the hydrolysis of the haloalkene-derived mercapturates S-(1,2-dichlorovinyl)-N-acetyl-L-cysteine, S-(1,2,3,4,4-pentachloro-1,3-butadienyl)-N-acetyl-L-cysteine, and S-(2,2-dibromo-1,1-difluoroethyl)-N-acetyl-L-cysteine. The substrate selectivity and amino acid sequence of the purified rat kidney acylase were studied. Although the sequence of the purified rat kidney acylase was somewhat identical with that of aspartoacylase, it did not catalyze the hydrolysis of N-acetyl-L-aspartate.

  DOI：

  10.1021/tx990090p
• 作为产物：
  描述：

  N-乙酰-L-半胱氨酸 、 三氯乙烯 在 1,5-二氮杂双环[4.3.0]壬-5-烯 作用下， 以 二甲基亚砜 为溶剂， 反应 3.0h， 以19.3%的产率得到(2R)-2-乙酰氨基-3-(2,2-二氯乙烯基硫基)丙酸
  参考文献：
  名称：

  通过细胞色素P450 3A对源自三氯乙烯和四氯乙烯的硫醇酸进行硫酸氧化：除脱乙酰基作用和半胱氨酸共轭β-裂合酶介导的裂解以外，还有生物活化反应。

  摘要：

  在本研究中，我们调查了由N-乙酰基-S-（1,2,2-三氯乙烯基）-L-半胱氨酸（N-Ac-TCVC），N-乙酰基-S-（1,2-二氯乙烯基）形成亚砜的情况）-L-半胱氨酸（N-Ac-1,2-DCVC）和N-乙酰基-S-（2,2-二氯乙烯基）-L-半胱氨酸（N-Ac-2,2-DCVC）谷胱甘肽对三氯乙烯和四氯乙烯的生物活化作用。第一个目的是阐明与这些氧化反应有关的酶。N-Ac-TCVC，N-Ac-1,2-DCVC和N-Ac-2,2-DCVC主要（如果非排他性地）被未经处理的雄性大鼠肝微粒体中的细胞色素P450酶氧化为相应的亚砜，因为通过热灭活实验和使用正辛胺无法证明含黄素的单加氧酶（FMO）的作用。当使用苯巴比妥和地塞米松预处理的雄性大鼠的肝微粒体以及地塞米松预处理的雌性大鼠的肝微粒体时，亚砜氧化速率增加，而未处理的雌性大鼠的肝微粒体中未观察到亚砜形成，表明细胞色素P450 3A参与其中。此外，曲雷霉素，一种细胞色素P450

  DOI：

  10.1021/tx950075u

文献信息

• Sulfoxidation of Mercapturic Acids Derived from Tri- and Tetrachloroethene by Cytochromes P450 3A:  A Bioactivation Reaction in Addition to Deacetylation and Cysteine Conjugate β-Lyase Mediated Cleavage
  作者：Michael Werner、Gerhard Birner、Wolfgang Dekant

  DOI：10.1021/tx950075u

  日期：1996.1.1

  2-DCVC are oxidized to the corresponding sulfoxides mainly, if not exclusively, by cytochrome P450 enzymes in liver microsomes of untreated male rats, since no role for the flavin-containing monooxygenase (FMO) could be demonstrated by heat inactivation experiments and by the use of n-octylamine. The sulfoxidation rates were increased when using liver microsomes of phenobarbital and dexamethasone pretreated

  在本研究中，我们调查了由N-乙酰基-S-（1,2,2-三氯乙烯基）-L-半胱氨酸（N-Ac-TCVC），N-乙酰基-S-（1,2-二氯乙烯基）形成亚砜的情况）-L-半胱氨酸（N-Ac-1,2-DCVC）和N-乙酰基-S-（2,2-二氯乙烯基）-L-半胱氨酸（N-Ac-2,2-DCVC）谷胱甘肽对三氯乙烯和四氯乙烯的生物活化作用。第一个目的是阐明与这些氧化反应有关的酶。N-Ac-TCVC，N-Ac-1,2-DCVC和N-Ac-2,2-DCVC主要（如果非排他性地）被未经处理的雄性大鼠肝微粒体中的细胞色素P450酶氧化为相应的亚砜，因为通过热灭活实验和使用正辛胺无法证明含黄素的单加氧酶（FMO）的作用。当使用苯巴比妥和地塞米松预处理的雄性大鼠的肝微粒体以及地塞米松预处理的雌性大鼠的肝微粒体时，亚砜氧化速率增加，而未处理的雌性大鼠的肝微粒体中未观察到亚砜形成，表明细胞色素P450 3A参与其中。此外，曲雷霉素，一种细胞色素P450
• Acylase-Catalyzed Deacetylation of Haloalkene-Derived Mercapturates
  作者：Vinita Uttamsingh、M. W. Anders

  DOI：10.1021/tx990090p

  日期：1999.10.1

  Mercapturates (S-substituted N-acetyl-L-cysteines) are terminal metabolites formed by the glutathione-dependent metabolism of electrophilic xenobiotics, including haloalkenes. Acylases catalyze the hydrolysis of N-acyl-L-amino acids, including many xenobiotic-derived mercapturates, to give fatty acids and amino acids as products. Although several acylases have been identified, the acylases that catalyze the deacetylation of the haloalkene-derived mercapturates have not been identified and characterized. Acylase I catalyzes the deacetylation of some haloalkene-derived mercapturates, including S-(1,1,2,2-tetrafluoroethyl)-N-acetyl-L-cysteine, S-(2-chloro-1,1,2-trifluoroethyl)-N-acetyl-cysteine, and S-(2-bromo-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine [Uttamsingh, V., et al. (1998) Chem. Res. Toxicol. 11, 800-809]. In the studies presented here, we identified a rat kidney acylase that catalyzed the hydrolysis of the haloalkene-derived mercapturates S-(1,2-dichlorovinyl)-N-acetyl-L-cysteine, S-(1,2,3,4,4-pentachloro-1,3-butadienyl)-N-acetyl-L-cysteine, and S-(2,2-dibromo-1,1-difluoroethyl)-N-acetyl-L-cysteine. The substrate selectivity and amino acid sequence of the purified rat kidney acylase were studied. Although the sequence of the purified rat kidney acylase was somewhat identical with that of aspartoacylase, it did not catalyze the hydrolysis of N-acetyl-L-aspartate.