Acetic acid (2R,3R,4R,5S,6R)-3-acetylamino-5-[(2R,4aR,6S,7R,8R,8aS)-8-benzyloxy-7-(3,4-dimethyl-2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-6-yloxy]-6-benzyloxymethyl-2-methoxy-tetrahydro-pyran-4-yl ester | 666728-57-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: Acetic acid (2R,3R,4R,5S,6R)-3-acetylamino-5-[(2R,4aR,6S,7R,8R,8aS)-8-benzyloxy-7-(3,4-dimethyl-2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-6-yloxy]-6-benzyloxymethyl-2-methoxy-tetrahydro-pyran-4-yl ester
• CAS: 666728-57-0
• 化学式: C₄₄H₅₀N₂O₁₃
• 分子量: 814.887
• InChiKey: OZHLNUVIOHIREO-MZFHACMUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.89
• 重原子数：
  59.0
• 可旋转键数：
  14.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  166.62
• 氢给体数：
  1.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  Acetic acid (2R,3R,4R,5S,6R)-3-acetylamino-5-[(2R,4aR,6S,7R,8R,8aS)-8-benzyloxy-7-(3,4-dimethyl-2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-6-yloxy]-6-benzyloxymethyl-2-methoxy-tetrahydro-pyran-4-yl ester 在 吡啶 、 sodium hydroxide 、 4 Angstroem molecular seives 、 sodium methylate 、 sodium hydride 作用下， 以 1,4-二氧六环 、 甲醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 22.5h， 生成
  参考文献：
  名称：

  Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria

  摘要：

  The major constituent of the bacterial cell wall, peptidoglycan, is comprised of repeating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide. Penicillin-binding proteins (PBPs) are involved in the final stages of bacterial cell wall assembly. Two activities for PBPs are the cross-linking of the cell wall, carried out by DD-transpeptidases, and the DD-peptidase activity, that removes the terminal D-Ala residue from peptidoglycan. The DD-peptidase activity moderates the extent of the cell wall cross-linking. There exists a balance between the two activities that is critical for the well-being of bacterial cells. We have cloned and purified PBP5 of Escherichia coli. The membrane anchor of this protein was removed, and the enzyme was obtained as a soluble protein. Two fragments of the polymeric cell wall of Gram-negative bacteria (compounds 5 and 6) were synthesized. These molecules served as substrates for PBP5. The products of the reactions of PBP5 and compounds 5 and 6 were isolated and were shown to be D-Ala and the fragments of the substrates minus the terminal D-Ala. The kinetic parameters for these enzymic reactions were evaluated. PBP5 would appear to have the potential for turnover of as many as 1.4 million peptidoglycan strands within a single doubling time (i.e., generation) of E. coli.

  DOI：

  10.1021/jo035397e
• 作为产物：
  描述：

  tert-butyldimethylsilyl 4,6-O-benzylidene-2-deoxy-2-dimethylmaleoyl-β-D-glucopyranoside 在 三氟甲磺酸 、 三氟甲磺酸三甲基硅酯 、 4 A molecular sieve 、 四丁基氟化铵 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 四氢呋喃 、 正己烷 、 二氯甲烷 为溶剂， 反应 7.0h， 生成 Acetic acid (2R,3R,4R,5S,6R)-3-acetylamino-5-[(2R,4aR,6S,7R,8R,8aS)-8-benzyloxy-7-(3,4-dimethyl-2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-6-yloxy]-6-benzyloxymethyl-2-methoxy-tetrahydro-pyran-4-yl ester
  参考文献：
  名称：

  Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria

  摘要：

  The major constituent of the bacterial cell wall, peptidoglycan, is comprised of repeating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide. Penicillin-binding proteins (PBPs) are involved in the final stages of bacterial cell wall assembly. Two activities for PBPs are the cross-linking of the cell wall, carried out by DD-transpeptidases, and the DD-peptidase activity, that removes the terminal D-Ala residue from peptidoglycan. The DD-peptidase activity moderates the extent of the cell wall cross-linking. There exists a balance between the two activities that is critical for the well-being of bacterial cells. We have cloned and purified PBP5 of Escherichia coli. The membrane anchor of this protein was removed, and the enzyme was obtained as a soluble protein. Two fragments of the polymeric cell wall of Gram-negative bacteria (compounds 5 and 6) were synthesized. These molecules served as substrates for PBP5. The products of the reactions of PBP5 and compounds 5 and 6 were isolated and were shown to be D-Ala and the fragments of the substrates minus the terminal D-Ala. The kinetic parameters for these enzymic reactions were evaluated. PBP5 would appear to have the potential for turnover of as many as 1.4 million peptidoglycan strands within a single doubling time (i.e., generation) of E. coli.

  DOI：

  10.1021/jo035397e