Monoglucosyl-(2,3-dihydroxybenzoylserine)3 | 880760-20-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: Monoglucosyl-(2,3-dihydroxybenzoylserine)3
• 英文别名: (2S)-3-[(2S)-2-[(2,3-dihydroxybenzoyl)amino]-3-[(2S)-2-[(2,3-dihydroxybenzoyl)amino]-3-hydroxypropanoyl]oxypropanoyl]oxy-2-[[2,3-dihydroxy-5-[(2S,3R,4R,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]benzoyl]amino]propanoic acid
• CAS: 880760-20-3
• 化学式: C₃₆H₃₉N₃O₂₁
• 分子量: 849.713
• InChiKey: BVNRZRVHEIZRPP-AEZKMRPASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  60
• 可旋转键数：
  18
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  409
• 氢给体数：
  15
• 氢受体数：
  21

反应信息

• 作为反应物：
  描述：

  Monoglucosyl-(2,3-dihydroxybenzoylserine)3 在 MceD protein 作用下， 以 水 为溶剂， 生成 (S)-2-(2,3-Dihydroxy-benzoylamino)-3-hydroxy-propionic acid (S)-2-carboxy-2-[2,3-dihydroxy-5-((2S,3R,4R,5S,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yl)-benzoylamino]-ethyl ester
  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
• 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) 在 MceD protein 作用下， 以 水 、 二甲基亚砜 为溶剂， 反应 0.33h， 生成 (S)-2-(2,3-Dihydroxy-benzoylamino)-3-hydroxy-propionic acid (S)-2-carboxy-2-[2,3-dihydroxy-5-((2S,3R,4R,5S,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yl)-benzoylamino]-ethyl ester 、 Monoglucosyl-(2,3-dihydroxybenzoylserine)3
  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