N-Acetylseleno-L-methionine

• 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-Acetylseleno-L-methionine
• 英文别名: N-Acetyl-L-selenomethionin；(2S)-2-acetamido-4-methylselanylbutanoic acid
• 化学式: C₇H₁₃NO₃Se
• 分子量: 238.145
• InChiKey: HUQQDUJBDSJFKN-LURJTMIESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.14
• 重原子数：
  12
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  66.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-Acetylseleno-L-methionine 在 pig kidney acylase I 作用下， 以 phosphate buffer 为溶剂， 反应 0.17h， 生成 L-硒代蛋氨酸
  参考文献：
  名称：

  Acylase I-Catalyzed Deacetylation of N-Acetyl-l-cysteine and S-Alkyl-N-acetyl-l-cysteines

  摘要：

  The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography, gel-filtration column chromatography, and hydrophobic interaction column chromatography. Acylase activity with NAC and N-acetyl-L-methionine (NAM), a known substrate for acylase I, as substrates coeluted during all chromatographic steps. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the protein was purified to near homogeneity and had a subunit M-r of 43 000, which is identical with the M-r of acylase I from porcine kidney and bovine liver. n-Butylmalonic acid was a slow-binding inhibitor of acylase I and inhibited the deacetylation of NAC with a K-i of 192 +/- 27 mu M These results show that acylase I catalyzes the deacetylation of NAG. The acylase I-catalyzed deacetylation of a range of S-alkyl-N-acetyl-L-cysteines, their carbon and oxygen analogues, and the selenium analogue of NAM was also studied with porcine kidney acylase I. The specific activity of the acylase I-catalyzed deacetylation of these substrates was related to their calculated molar volumes and lag P values. The S-alkyl-N-acetyl-L-cysteines with short (C-0-C-3) and unbranched S-alkyl substituents were good acylase I substrates, whereas the S-alkyl-N-acetyl-L-cysteines with long (>C-3) and branched S-alkyl substituents were poor acylase I substrates. The carbon and oxygen analogues of S-methyl-N-acetyl-L-cysteine and the carbon analogue of S-ethyl-N-acetyl-L-cysteine were poor acylase I substrates, whereas the selenium analogue of NAM was a good acylase I substrate.

  DOI：

  10.1021/tx980018b
• 作为产物：
  描述：

  乙酸五氟苯酯 、 L-硒代蛋氨酸 以 N,N-二甲基甲酰胺 为溶剂， 生成 N-Acetylseleno-L-methionine
  参考文献：
  名称：

  Acylase I-Catalyzed Deacetylation of N-Acetyl-l-cysteine and S-Alkyl-N-acetyl-l-cysteines

  摘要：

  The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography, gel-filtration column chromatography, and hydrophobic interaction column chromatography. Acylase activity with NAC and N-acetyl-L-methionine (NAM), a known substrate for acylase I, as substrates coeluted during all chromatographic steps. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the protein was purified to near homogeneity and had a subunit M-r of 43 000, which is identical with the M-r of acylase I from porcine kidney and bovine liver. n-Butylmalonic acid was a slow-binding inhibitor of acylase I and inhibited the deacetylation of NAC with a K-i of 192 +/- 27 mu M These results show that acylase I catalyzes the deacetylation of NAG. The acylase I-catalyzed deacetylation of a range of S-alkyl-N-acetyl-L-cysteines, their carbon and oxygen analogues, and the selenium analogue of NAM was also studied with porcine kidney acylase I. The specific activity of the acylase I-catalyzed deacetylation of these substrates was related to their calculated molar volumes and lag P values. The S-alkyl-N-acetyl-L-cysteines with short (C-0-C-3) and unbranched S-alkyl substituents were good acylase I substrates, whereas the S-alkyl-N-acetyl-L-cysteines with long (>C-3) and branched S-alkyl substituents were poor acylase I substrates. The carbon and oxygen analogues of S-methyl-N-acetyl-L-cysteine and the carbon analogue of S-ethyl-N-acetyl-L-cysteine were poor acylase I substrates, whereas the selenium analogue of NAM was a good acylase I substrate.

  DOI：

  10.1021/tx980018b

文献信息

• Carvacrol Codrugs: A New Approach in the Antimicrobial Plan
  作者：Ivana Cacciatore、Mara Di Giulio、Erika Fornasari、Antonio Di Stefano、Laura Serafina Cerasa、Lisa Marinelli、Hasan Turkez、Emanuela Di Campli、Soraya Di Bartolomeo、Iole Robuffo、Luigina Cellini

  DOI：10.1371/journal.pone.0120937

  日期：——

  bacterial infections led to identify alternative strategies for a novel therapeutic approach. In this study, we synthesized ten carvacrol codrugs - obtained linking the carvacrol hydroxyl group to the carboxyl moiety of sulphur-containing amino acids via an ester bond - to develop novel compounds with improved antimicrobial and antibiofilm activities and reduced toxicity respect to carvacrol alone. METHOD All

  目的抗生素耐药性细菌感染的流行率不断上升，从而确定了一种新的治疗方法的替代策略。在这项研究中，我们合成了十种香芹酚前药-通过酯键将香芹酚羟基与含硫氨基酸的羧基部分连接在一起-开发出具有改善的抗微生物和抗生物膜活性以及相对于单独的香芹酚而言毒性降低的新型化合物。方法使用肉汤微量稀释法，针对代表性的革兰氏阳性（金黄色葡萄球菌和表皮葡萄球菌），革兰氏阴性（大肠杆菌和铜绿假单胞菌）细菌菌株和白色念珠菌筛选所有香芹酚前药。结果结果表明香芹酚共药4具有最显着的抗菌活性增强，其MIC和MBC值等于2。除铜绿假单胞菌ATCC 9027（MIC和MBC值分别等于5 mg / mL和10 mg / mL）外，所有细菌菌株均为5 mg / mL。所有香芹酚前药1-10对白色念珠菌ATCC 10231均显示出良好的抗真菌活性。细胞毒性测定表明，除香熏药物8和9外，新型香芹酚前药在其MIC值下均不会产生人血溶血。特