N-acetyl-4,6-di-O-acetyl-1-(O-hydroxy-1H-imidazol-1-ylphosphinyl)muramic acid methyl ester triethylamine salt | 1313490-30-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-acetyl-4,6-di-O-acetyl-1-(O-hydroxy-1H-imidazol-1-ylphosphinyl)muramic acid methyl ester triethylamine salt
• CAS: 1313490-30-0
• 化学式: C₆H₁₅N*C₁₉H₂₈N₃O₁₂P
• 分子量: 622.61
• InChiKey: OSMPOLBDJHWYCR-FUGYBOJVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.87
• 重原子数：
  42.0
• 可旋转键数：
  13.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.72
• 拓扑面积：
  194.05
• 氢给体数：
  2.0
• 氢受体数：
  14.0

反应信息

• 作为反应物：
  描述：

  N-acetyl-4,6-di-O-acetyl-1-(O-hydroxy-1H-imidazol-1-ylphosphinyl)muramic acid methyl ester triethylamine salt 在 lithium hydroxide monohydrate 、 1-甲基氯化咪唑鎓 作用下， 以 四氢呋喃 、 甲醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 14.0h， 生成 N-acetyl-1-[P'-[(2Z,6Z,10Z,14Z,18E,22E)-3,7,11,15,19,23,27-heptamethyl-2,6,10,14,18,22,26-octacosaheptaen-1-yl]diammonium diphosphate]muramic acid
  参考文献：
  名称：

  N-Methylimidazolium chloride-catalyzed pyrophosphate formation: Application to the synthesis of Lipid I and NDP-sugar donors

  摘要：

  N-Methylimidazolium chloride is found to catalyze a coupling reaction between monophosphates and activated phosphorous-nitrogen intermediates such as a phosphorimidazolide and phosphoromorpholidate to form biologically important unsymmetrical pyrophosphate diesters. The catalyst is much more active, cheaper, and less explosive than 1H-tetrazole, known as the best catalyst for the pyrophosphate formation over a decade. The mild and neutral reaction conditions are compatible with allylic pyrophosphate formation in Lipid I syntheisis. (31)P NMR experiments suggest that the catalyst acts not only as an acid but also as a nucleophile to form cationic and electrophilic phosphor-N-methylimidazolide intermediates in the pyrophosphate formation. (c) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.04.061
• 作为产物：
  描述：

  、 N,N'-羰基二咪唑 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 N-acetyl-4,6-di-O-acetyl-1-(O-hydroxy-1H-imidazol-1-ylphosphinyl)muramic acid methyl ester triethylamine salt
  参考文献：
  名称：

  Transpeptidase-Mediated Incorporation of d-Amino Acids into Bacterial Peptidoglycan

  摘要：

  The beta-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse D-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical D-amino acids can be introduced into the bacterial cell wall.

  DOI：

  10.1021/ja2040656