| 1000183-94-7

• 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
• CAS: 1000183-94-7
• 化学式: C₆₅H₈₅N₁₃O₃₇
• 分子量: 1640.45
• InChiKey: YHVJUXVMCOCLRC-FEBFPLPOSA-N

物化性质

• 沸点：
  2093.2±65.0 °C(Predicted)
• 密度：
  1.72±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -15.37
• 重原子数：
  115.0
• 可旋转键数：
  35.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  813.33
• 氢给体数：
  29.0
• 氢受体数：
  38.0

反应信息

• 作为产物：
  描述：

  N,N'-((3S,7S,11S)-11-(2,3-dihydroxy-5-((2S,3R,4R,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)benzamido)-2,6,10-trioxo-1,5,9-trioxacyclododecane-3,7-diyl)bis(2,3-dihydroxybenzamide) 、 SATSSSGSGS 在 三(2-羰基乙基)磷盐酸盐 、 magnesium chloride 作用下， 以 水 为溶剂， 反应 7.25h， 生成 、
  参考文献：
  名称：

  Biosynthetic Tailoring of Microcin E492m:  Post-translational Modification Affords an Antibacterial Siderophore−Peptide Conjugate

  摘要：

  The present work reveals that four proteins, MceCDIJ, encoded by the MccE492 gene cluster are responsible for the remarkable post-translational tailoring of microcin E492 (MccE492), an 84-residue protein toxin secreted by Klebsiella pheumonaie RYC492 that targets neighboring Gram-negative species. This modification results in attachment of a linearized and monoglycosylated derivative of enterobactin, a nonribosomal peptide and iron scavenger (siderophore), to the MccE492m C-terminus. MceC and MceD derivatize enterobactin by C-glycosylation at the C5 position of a N-(2,3-dihydroxybenzoyl)serine (DHB-Ser) moiety and regiospecific hydrolysis of an ester linkage in the trilactone scaffold, respectively. Mcel and MceJ form a protein complex that attaches C-glycosylated enterobactins to the C-terminal serine residue of both a C-10 model peptide and full-length MccE492. In the enzymatic product, the C-terminal serine residue is covalently attached to the C4'oxygen of the glucose moiety. Nonenzymatic and base-catalyzed migration of the peptide to the C6' position affords the C6' glycosyl ester linkage observed in the mature toxin, MccE492m, isolated from bacterial cultures.

  DOI：

  10.1021/ja074650f