N^ε-(methylthiocarbamoyl)lysine | 160364-23-8

• 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: N^ε-(methylthiocarbamoyl)lysine
• CAS: 160364-23-8
• 化学式: C₈H₁₇N₃O₂S
• 分子量: 219.308
• InChiKey: ZRPGWKQIWAUACK-LURJTMIESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.34
• 重原子数：
  14.0
• 可旋转键数：
  6.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  87.38
• 氢给体数：
  4.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  N^ε-(methylthiocarbamoyl)lysine 生成 6-isothiocyanato-L-norleucine
  参考文献：
  名称：

  Characterization of Protein Adducts Produced by N-Methyldithiocarbamate and N-Methyldithiocarbamate Esters

  摘要：

  The toxicity of N-methyldithiocarbamate may be mediated through decomposition to more biologically active compounds. Two principal products, CS2 and methyl isothiocyanate, have the potential to interact covalently with macromolecules in biological systems. In this investigation the ability of N-methyldithiocarbamate to generate methyl isothiocyanate and CS2 under physiological conditions resulting in acylation and covalent cross-linking of proteins was examined using C-13 NMR and GC/MS. Two N-methyldithiocarbamate esters, S-methyl N-methyldithiocarbamate and (N-acetyl-S-methylthiocarbamoyl)cysteine were also investigated to evaluate the acylating ability of sulfhydryl conjugates of N-methyldithiocarbamate. The predominant and most stable adduct produced by the free dithiocarbamate and its S-substituted esters was methylthiourea on epsilon-lysyl and N-terminal alpha-amino groups. Derivatization on N-terminal amino groups progressed more rapidly for the dithiocarbamate than for its mercapturate. Methylurea protein adducts were also produced by the dithiocarbamate and its esters, suggesting production of methyl isocyanate in the decomposition of N-methyldithiocarbamate. Covalent cross-linking of beta-lactoglobulin by N-methyldithiocarbamate resulting from its decomposition to CS2 was observed using denaturing polyacrylamide gel electrophoresis. These results demonstrate the ability of a monoalkyldithiocarbamate to acylate protein amino groups and effect covalent cross-linking. These processes represent molecular mechanisms that may contribute to the toxicity of this class of compounds.

  DOI：

  10.1021/tx00044a011
• 作为产物：
  描述：

  N-乙酰-L-赖氨酸 在 盐酸 、 sodium hydroxide 作用下， 以 水 、 异丙醇 为溶剂， 反应 32.0h， 生成 N^ε-(methylthiocarbamoyl)lysine
  参考文献：
  名称：

  Characterization of Protein Adducts Produced by N-Methyldithiocarbamate and N-Methyldithiocarbamate Esters

  摘要：

  The toxicity of N-methyldithiocarbamate may be mediated through decomposition to more biologically active compounds. Two principal products, CS2 and methyl isothiocyanate, have the potential to interact covalently with macromolecules in biological systems. In this investigation the ability of N-methyldithiocarbamate to generate methyl isothiocyanate and CS2 under physiological conditions resulting in acylation and covalent cross-linking of proteins was examined using C-13 NMR and GC/MS. Two N-methyldithiocarbamate esters, S-methyl N-methyldithiocarbamate and (N-acetyl-S-methylthiocarbamoyl)cysteine were also investigated to evaluate the acylating ability of sulfhydryl conjugates of N-methyldithiocarbamate. The predominant and most stable adduct produced by the free dithiocarbamate and its S-substituted esters was methylthiourea on epsilon-lysyl and N-terminal alpha-amino groups. Derivatization on N-terminal amino groups progressed more rapidly for the dithiocarbamate than for its mercapturate. Methylurea protein adducts were also produced by the dithiocarbamate and its esters, suggesting production of methyl isocyanate in the decomposition of N-methyldithiocarbamate. Covalent cross-linking of beta-lactoglobulin by N-methyldithiocarbamate resulting from its decomposition to CS2 was observed using denaturing polyacrylamide gel electrophoresis. These results demonstrate the ability of a monoalkyldithiocarbamate to acylate protein amino groups and effect covalent cross-linking. These processes represent molecular mechanisms that may contribute to the toxicity of this class of compounds.

  DOI：

  10.1021/tx00044a011

文献信息

• Characterization of Protein Adducts Produced by N-Methyldithiocarbamate and N-Methyldithiocarbamate Esters
  作者：William M. Valentine、Venkataraman Amarnath、Kalyani Amarnath、Doyle G. Graham

  DOI：10.1021/tx00044a011

  日期：1995.3

  The toxicity of N-methyldithiocarbamate may be mediated through decomposition to more biologically active compounds. Two principal products, CS2 and methyl isothiocyanate, have the potential to interact covalently with macromolecules in biological systems. In this investigation the ability of N-methyldithiocarbamate to generate methyl isothiocyanate and CS2 under physiological conditions resulting in acylation and covalent cross-linking of proteins was examined using C-13 NMR and GC/MS. Two N-methyldithiocarbamate esters, S-methyl N-methyldithiocarbamate and (N-acetyl-S-methylthiocarbamoyl)cysteine were also investigated to evaluate the acylating ability of sulfhydryl conjugates of N-methyldithiocarbamate. The predominant and most stable adduct produced by the free dithiocarbamate and its S-substituted esters was methylthiourea on epsilon-lysyl and N-terminal alpha-amino groups. Derivatization on N-terminal amino groups progressed more rapidly for the dithiocarbamate than for its mercapturate. Methylurea protein adducts were also produced by the dithiocarbamate and its esters, suggesting production of methyl isocyanate in the decomposition of N-methyldithiocarbamate. Covalent cross-linking of beta-lactoglobulin by N-methyldithiocarbamate resulting from its decomposition to CS2 was observed using denaturing polyacrylamide gel electrophoresis. These results demonstrate the ability of a monoalkyldithiocarbamate to acylate protein amino groups and effect covalent cross-linking. These processes represent molecular mechanisms that may contribute to the toxicity of this class of compounds.