linear enterobactin | 30414-16-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: linear enterobactin
• 英文别名: enterobactin；N,N',N''-tris(2,3-dihydroxybenzoyl)-O-L-seryl-O-L-seryl L-serine；(2S)-2-[(2,3-dihydroxybenzoyl)amino]-3-[(2S)-2-[(2,3-dihydroxybenzoyl)amino]-3-[(2S)-2-[(2,3-dihydroxybenzoyl)amino]-3-hydroxypropanoyl]oxypropanoyl]oxypropanoic acid
• CAS: 30414-16-5
• 化学式: C₃₀H₂₉N₃O₁₆
• 分子量: 687.571
• InChiKey: NTWRWGRCGVKQNS-BZSNNMDCSA-N

物化性质

• 沸点：
  1034.7±65.0 °C(Predicted)
• 密度：
  1.628±0.06 g/cm3(Predicted)
• 溶解度：
  DMSO：可溶；甲醇：可溶

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  49
• 可旋转键数：
  16
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  319
• 氢给体数：
  11
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  凝乳酶 在 MceD protein 作用下， 以 水 、 二甲基亚砜 为溶剂， 反应 0.45h， 生成 linear enterobactin
  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

文献信息

• Heavy-Metal Trojan Horse: Enterobactin-Directed Delivery of Platinum(IV) Prodrugs to <i>Escherichia coli</i>
  作者：Chuchu Guo、Elizabeth M. Nolan

  DOI：10.1021/jacs.2c03324

  日期：2022.7.20

  design of new antibiotics. Drug repurposing is a promising strategy for expanding the antibiotic repertoire. In this study, we repurpose the clinically approved anticancer agent cisplatin into a targeted antibiotic by conjugating its Pt(IV) prodrug to enterobactin (Ent), a triscatecholate siderophore employed by Enterobacteriaceae for iron (Fe) acquisition. The l-Ent-Pt(IV) conjugate (l-EP) exhibits

  无法治疗的微生物感染的全球危机需要设计新的抗生素。药物再利用是扩大抗生素库的一个有前途的策略。在这项研究中，我们通过将其 Pt(IV) 前药与肠杆菌素 (Ent) 缀合，将临床批准的抗癌剂顺铂重新用于靶向抗生素，肠杆菌素是肠杆菌科用于获取铁 (Fe) 的三儿茶酚酸铁载体。l -Ent -Pt(IV) 缀合物 ( l -EP) 对大肠杆菌K12 和尿路致病性分离株大肠杆菌CFT073 表现出抗菌活性。与顺铂类似，l -EP 在大肠杆菌中引起丝状形态并引发溶原菌裂解。对 Ent 转运蛋白缺陷的大肠杆菌突变体的研究表明，Ent 介导将l -EP递送到大肠杆菌细胞质中，其中 Pt(IV) 前药的还原释放顺铂弹头，导致大肠杆菌的生长抑制和丝状化。大肠杆菌。用其对映体取代 Ent 得到d -Ent-Pt(IV) 缀合物 ( d -EP)，其显示出增强的抗菌活性，大概是因为d -Ent 不能被 Ent 酯酶水解，因此
• Suppression of Linear Side Products by Macromolecular Crowding in Nonribosomal Enterobactin Biosynthesis
  作者：Zu-Feng Guo、Ming Jiang、Suilan Zheng、Zhihong Guo

  DOI：10.1021/ol7030153

  日期：2008.2.1

  Nonribosomal enterobactin synthetase of Escherichia coli was found to prematurely release a large amount of linear precursors in an in vitro reconstitution. However, these side products are suppressed to negligible levels by polymeric cosolvents that create macromolecular crowding, a prominent feature of the intracellular environment. These findings show that macromolecular crowding is essential to normal functioning of the nonribosomal peptide synthetase and suggest that it may be crucial to biotechnological utilization of similar enzyme systems.
• Structural change of the enterobactin synthetase in crowded solution and its relation to crowding-enhanced product specificity in nonribosomal enterobactin biosynthesis
  作者：Zu-Feng Guo、Ming Jiang、Suilan Zheng、Zhihong Guo

  DOI：10.1016/j.bmcl.2010.05.051

  日期：2010.7

  Significant conformational change is detected by circular dichroism and fluorimetry for the major component of the enterobactin synthetase in crowded solutions mimicking the intracellular environment. The structural change correlates well with the extent of the crowding-induced side product suppression in nonribosomal enterobactin synthesis. In contrast, protein-stabilizing solvophobic agents such as glycerol have no effect on the formation of side products, excluding crowding-induced protein stability as a cause for the observed enhancement of the product specificity of the synthetase. These results strongly support that macromolecular crowding is an indispensable physiological factor for normal functioning of the nonribosomal enterobactin synthetase by altering the active sites to increase its product specificity. (c) 2010 Elsevier Ltd. All rights reserved.