S-(2-(3-acetamidopropanamido)ethyl) ethanethioate | 502484-68-6

• 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-(3-acetamidopropanamido)ethyl) ethanethioate
• 英文别名: N-acetyl-β-alanine-(2-acetylsulfanyl-ethylamide)；S-Acetyl-N-(N-acetyl-β-alanyl)-cysteamin；1-[(N-Acetyl-β-alanyl)-amino]-2-acetylmercapto-aethan；N-Acetyl-β-alanin-(2-acetylmercapto-aethylamid)；3-acetylamino-N-(2-acetylthioethyl)propionamide；S-[2-(3-acetamidopropanoylamino)ethyl] ethanethioate
• CAS: 502484-68-6
• 化学式: C₉H₁₆N₂O₃S
• 分子量: 232.304
• InChiKey: DDDVINJUMQBWAD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.8
• 重原子数：
  15
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  chitotriose 、 S-(2-(3-acetamidopropanamido)ethyl) ethanethioate 在 peptidoglycan O-acetyltransferase B 作用下， 以 aq. buffer 为溶剂， 反应 2.0h， 生成
  参考文献：
  名称：

  Postsynthetic Modification of Bacterial Peptidoglycan Using Bioorthogonal N-Acetylcysteamine Analogs and Peptidoglycan O-Acetyltransferase B

  摘要：

  Bacteria have the natural ability to install protective postsynthetic modifications onto its bacterial peptidoglycan (PG), the coat woven into bacterial cell wall. Peptidoglycan O-acetyltransferase B (PatB) catalyzes the O-acetylation of PG in Gram (-) bacteria, which aids in bacterial survival, as it prevents autolysins such as lysozyme from cleaving the PG. We explored the mechanistic derails of PatB's acetylation function and determined that PatB has substrate specificity for bioorthgonal short N-acetyl cysteamine (SNAc) donors. A variety of functionality including azides and alkynes were installed on tri-N-acetylglucosamine (NAG)3, a PG mimic, as well as PG isolated from various Gram (+) and Gram () bacterial species. The bioorthogonal modifications protect the isolated PG against lysozyme degradation in vitro. We further demonstrate that this postsynthetic Modification of PG can be extended to use click chemistry to fluorescently label the mature PG in whole bacterial cells of Bacillus subtilis. Modifying PG postsynthetically can aid in the development of antibiotics and immune modulators by expanding the understanding of how PG is processed by lytic enzymes.

  DOI：

  10.1021/jacs.7b06820
• 作为产物：
  描述：

  bis-{2-[(N-benzyloxycarbonyl-β-alanyl)-amino]-ethyl}-disulfide 在 氨 、 sodium 作用下， 生成 S-(2-(3-acetamidopropanamido)ethyl) ethanethioate
  参考文献：
  名称：

  Studies on Thioesters Related to Coenzyme A. A Kinetic Study of Aminolysis and Hydrolysis of β-(N-Methylacetamino)-ethyl Thioacetate, N,S-Diacetylaletheine and γ-Acetaminopropyl Thioacetate¹

  摘要：

  DOI：

  10.1021/ja01593a023

文献信息

• 145. Coenzyme a. Part V. A new and convenient synthesis of pantetheine (Lactobacillus bulgaricus factor)
  作者：J. Baddiley、E. M. Thain

  DOI：10.1039/jr9520000800

  日期：——
• 754. Coenzyme A. Part IV. Derivatives of 2-acetylthioethylamine as acetylating agents
  作者：J. Baddiley、E. M. Thain

  DOI：10.1039/jr9510003425

  日期：——
• US4552765A
  申请人：——

  公开号：US4552765A

  公开（公告）日：1985-11-12
• Studies on Thioesters Related to Coenzyme A. A Kinetic Study of Aminolysis and Hydrolysis of β-(N-Methylacetamino)-ethyl Thioacetate, N,S-Diacetylaletheine and γ-Acetaminopropyl Thioacetate¹
  作者：D. Stanley Tarbell、Donald P. Cameron

  DOI：10.1021/ja01593a023

  日期：1956.6
• Postsynthetic Modification of Bacterial Peptidoglycan Using Bioorthogonal <i>N</i>-Acetylcysteamine Analogs and Peptidoglycan <i>O</i>-Acetyltransferase B
  作者：Yiben Wang、Klare M. Lazor、Kristen E. DeMeester、Hai Liang、Tyler K. Heiss、Catherine L. Grimes

  DOI：10.1021/jacs.7b06820

  日期：2017.10.4

  Bacteria have the natural ability to install protective postsynthetic modifications onto its bacterial peptidoglycan (PG), the coat woven into bacterial cell wall. Peptidoglycan O-acetyltransferase B (PatB) catalyzes the O-acetylation of PG in Gram (-) bacteria, which aids in bacterial survival, as it prevents autolysins such as lysozyme from cleaving the PG. We explored the mechanistic derails of PatB's acetylation function and determined that PatB has substrate specificity for bioorthgonal short N-acetyl cysteamine (SNAc) donors. A variety of functionality including azides and alkynes were installed on tri-N-acetylglucosamine (NAG)3, a PG mimic, as well as PG isolated from various Gram (+) and Gram () bacterial species. The bioorthogonal modifications protect the isolated PG against lysozyme degradation in vitro. We further demonstrate that this postsynthetic Modification of PG can be extended to use click chemistry to fluorescently label the mature PG in whole bacterial cells of Bacillus subtilis. Modifying PG postsynthetically can aid in the development of antibiotics and immune modulators by expanding the understanding of how PG is processed by lytic enzymes.