(2S)-2-乙酰氨基-5-氧代-戊酸 | 13074-21-0

• 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: (2S)-2-乙酰氨基-5-氧代-戊酸
• 英文名称: N-acetylglutamate-5-semialdehyde
• 英文别名: N-acetyl-L-glutamate 5-semialdehyde；(2S)-2-acetamido-5-oxopentanoic acid
• CAS: 13074-21-0
• 化学式: C₇H₁₁NO₄
• 分子量: 173.169
• InChiKey: BCPSFKBPHHBDAI-LURJTMIESA-N

物化性质

• 沸点：
  466.0±40.0 °C(Predicted)
• 密度：
  1.216±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  12
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  83.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2S)-2-乙酰氨基-5-氧代-戊酸 在 盐酸 、 水 、 sodium cyanoborohydride 作用下， 反应 12.0h， 生成 4-[[(4S)-4-amino-4-carboxybutyl]amino]benzoic acid
  参考文献：
  名称：

  Antioxidant and pro-oxidant actions of resveratrol on human serum albumin in the presence of toxic diabetes metabolites: Glyoxal and methyl-glyoxal

  摘要：

  Methylglyoxal (MGO) and glyoxal (GO) are attracting considerable attention because of their role in the onset of diabetes symptoms. Therefore, to comprehend the molecular fundamentals of their pathological actions is of the utmost importance. In this study, the molecular interactions between resveratrol (RES) and human serum albumin (HSA) and the ability of the stilbene to counteract the oxidative damage caused by pathological concentrations of MGO and GO to the human plasma protein, was assessed. The oxidation of Cys34 in HSA as well as the formation of specific protein semialdehydes AAS (alpha-aminoadipic), GGS (gamma-glutamic) and the accumulation of Advanced Glycation End-products (AGEs) was investigated. Resveratrol was found to neutralize both alpha-di-carbonyls by forming adducts detected by HESI-Orbitrap-MS. This antioxidant action was manifested in a significant reduction of AGEs. However, RES-alpha-dicarbonyl conjugates oxidized Cys34 and lysine, arginine and/or proline by a nucleophilic attack on SH and epsilon-NH groups in HSA. The formation of specific semialdehydes in HSA after incubation with GO and MGO at pathological concentrations was reported for the first time in this study, and may be used as early and specific biomarkers of the oxidative stress undergone by diabetic patients. The pro oxidative role of the RES-alpha-dicarbonyl conjugates should be further investigated to clarify whether this action leads to positive or harmful clinical consequences. The biological relevance of human protein carbonylation as a redox signaling mechanism and/or as a reflection of oxidative damage and disease should also be studied in future works.

  DOI：

  10.1016/j.bbagen.2018.06.007
• 作为产物：
  描述：

  (S)-2-乙酰氨基-5-氨基戊酸 在 egg shell membrane 作用下， 以 aq. phosphate buffer 为溶剂， 反应 24.0h， 生成 (2S)-2-乙酰氨基-5-氧代-戊酸
  参考文献：
  名称：

  Antioxidant and pro-oxidant actions of resveratrol on human serum albumin in the presence of toxic diabetes metabolites: Glyoxal and methyl-glyoxal

  摘要：

  Methylglyoxal (MGO) and glyoxal (GO) are attracting considerable attention because of their role in the onset of diabetes symptoms. Therefore, to comprehend the molecular fundamentals of their pathological actions is of the utmost importance. In this study, the molecular interactions between resveratrol (RES) and human serum albumin (HSA) and the ability of the stilbene to counteract the oxidative damage caused by pathological concentrations of MGO and GO to the human plasma protein, was assessed. The oxidation of Cys34 in HSA as well as the formation of specific protein semialdehydes AAS (alpha-aminoadipic), GGS (gamma-glutamic) and the accumulation of Advanced Glycation End-products (AGEs) was investigated. Resveratrol was found to neutralize both alpha-di-carbonyls by forming adducts detected by HESI-Orbitrap-MS. This antioxidant action was manifested in a significant reduction of AGEs. However, RES-alpha-dicarbonyl conjugates oxidized Cys34 and lysine, arginine and/or proline by a nucleophilic attack on SH and epsilon-NH groups in HSA. The formation of specific semialdehydes in HSA after incubation with GO and MGO at pathological concentrations was reported for the first time in this study, and may be used as early and specific biomarkers of the oxidative stress undergone by diabetic patients. The pro oxidative role of the RES-alpha-dicarbonyl conjugates should be further investigated to clarify whether this action leads to positive or harmful clinical consequences. The biological relevance of human protein carbonylation as a redox signaling mechanism and/or as a reflection of oxidative damage and disease should also be studied in future works.

  DOI：

  10.1016/j.bbagen.2018.06.007

文献信息

• Probing the Role of <i>N</i>-Acetyl-glutamyl 5-Phosphate, an Acyl Phosphate, in the Construction of the Azabicycle Moiety of the Azinomycins
  作者：Keshav K. Nepal、Rachel P. Lee、Yohannes H. Rezenom、Coran M. H. Watanabe

  DOI：10.1021/acs.biochem.5b00711

  日期：2015.7.28

  The azinomycins are potent antitumor agents produced by the soil bacterium Streptomyces sahachiroi and contain a novel aziridino[1,2-a]pyrrolidine core; its synthesis involves at least 14 steps. This study reports the first reconstitution of N-acetylglutamine semialdehyde formation by two enzymes encoded in the azinomycin biosynthetic gene cluster. The reaction proceeds through the formation of an acylphosphate and establishes N-acetyl-glutamyl 5-phosphate and N-acetylglutamine semialdehyde as intermediates in the complex biosynthesis of the aziridino[1,2-a]pyrrolidine moiety.

  阿齐霉素是由土壤细菌Streptomyces sahachiroi产生的强效抗肿瘤药物，含有新型氮丙啶[1,2-a]吡咯烷核心，其合成至少涉及14个步骤。本研究首次报道了由阿齐霉素生物合成基因簇编码的两个酶对N-乙酰谷氨酰胺半醛形成的重组。该反应通过形成酰基磷酸，并建立N-乙酰谷氨酰5-磷酸和N-乙酰谷氨酰胺半醛作为氮丙啶[1,2-a]吡咯烷部分复杂生物合成的中间体。
• Antioxidant and pro-oxidant actions of resveratrol on human serum albumin in the presence of toxic diabetes metabolites: Glyoxal and methyl-glyoxal
  作者：N.M.O. Arcanjo、C. Luna、M.S. Madruga、M. Estévez

  DOI：10.1016/j.bbagen.2018.06.007

  日期：2018.9

  Methylglyoxal (MGO) and glyoxal (GO) are attracting considerable attention because of their role in the onset of diabetes symptoms. Therefore, to comprehend the molecular fundamentals of their pathological actions is of the utmost importance. In this study, the molecular interactions between resveratrol (RES) and human serum albumin (HSA) and the ability of the stilbene to counteract the oxidative damage caused by pathological concentrations of MGO and GO to the human plasma protein, was assessed. The oxidation of Cys34 in HSA as well as the formation of specific protein semialdehydes AAS (alpha-aminoadipic), GGS (gamma-glutamic) and the accumulation of Advanced Glycation End-products (AGEs) was investigated. Resveratrol was found to neutralize both alpha-di-carbonyls by forming adducts detected by HESI-Orbitrap-MS. This antioxidant action was manifested in a significant reduction of AGEs. However, RES-alpha-dicarbonyl conjugates oxidized Cys34 and lysine, arginine and/or proline by a nucleophilic attack on SH and epsilon-NH groups in HSA. The formation of specific semialdehydes in HSA after incubation with GO and MGO at pathological concentrations was reported for the first time in this study, and may be used as early and specific biomarkers of the oxidative stress undergone by diabetic patients. The pro oxidative role of the RES-alpha-dicarbonyl conjugates should be further investigated to clarify whether this action leads to positive or harmful clinical consequences. The biological relevance of human protein carbonylation as a redox signaling mechanism and/or as a reflection of oxidative damage and disease should also be studied in future works.