S-(2,2-dibromo-1,1-difluoroethyl)-L-cysteine | 126637-65-8

• 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: S-(2,2-dibromo-1,1-difluoroethyl)-L-cysteine
• 英文别名: (2R)-2-amino-3-(2,2-dibromo-1,1-difluoroethyl)sulfanylpropanoic acid
• CAS: 126637-65-8
• 化学式: C₅H₇Br₂F₂NO₂S
• 分子量: 342.987
• InChiKey: XWMHGYJFIBTLLW-REOHCLBHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  13
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  88.6
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  S-(2,2-dibromo-1,1-difluoroethyl)-N-acetyl-L-cysteine 在 rat kidney acylase 作用下， 以 phosphate buffer 为溶剂， 反应 0.5h， 生成 S-(2,2-dibromo-1,1-difluoroethyl)-L-cysteine
  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

文献信息

• 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.