Ferric enterobactin ion | 61481-53-6

• 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: Ferric enterobactin ion
• 英文别名: 3-[[(3S,7S,11S)-7,11-bis[(2,3-dioxidobenzoyl)amino]-2,6,10-trioxo-1,5,9-trioxacyclododec-3-yl]carbamoyl]benzene-1,2-diolate;iron(3+)
• CAS: 61481-53-6
• 化学式: C₃₀H₂₁FeN₃O₁₅
• 分子量: 719.355
• InChiKey: NGILTSZTOFYVBF-UVJOBNTFSA-H

计算性质

• 辛醇/水分配系数(LogP)：
  -4.54
• 重原子数：
  49
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  305
• 氢给体数：
  3
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  Ferric enterobactin ion 、 水 生成 Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]₃ 、 氢(+1)阳离子
  参考文献：
  名称：

  肠埃希氏大肠杆菌K-12中肠螯合素及其铁配合物的酶水解。肠螯合酯酶的性质。

  摘要：

  为了解决先前报道之间的差异，已经研究了将肠螯合素（2,3-二羟基-N-苯甲酰基-L-丝氨酸的环状三聚体）水解为2,3-二羟基苯甲酰基丝氨酸的酶的性质。肠螯合酯酶以前据报道由两部分组成（O'Brien，IG，Cox，GB和Gibson，F.（1971）Biochim。Biophys。Acta 237，537-549），在不存在下具有完全活性所谓的A分量。先前描述的水解酶（Bryce，GF和Brot，N.（1972）生物化学11，1708-1715）能够分解肠螯合素，但不能分解其铁络合物铁-肠螯合铁蛋白，似乎与肠螯合素的B成分相同酯酶。对应于先前描述的组分B的单一组分肠螯合素酯酶，水解肠黏附素和肠铁黏附素。在使用的测定条件下，肠螯合素的水解速度比复合物快2.5倍。酶活性受到N-乙基马来酰亚胺的抑制，并在37摄氏度时迅速丧失。在铁-肠螯合素，肠螯合素，二硫苏糖醇或某些蛋白质组分的存在下，酶的活性得以稳定。

  DOI：

  10.1016/0005-2744(78)90216-4
• 作为产物：
  描述：

  凝乳酶 、 三氯化铁 以 盐酸 、 甲醇 、 水 为溶剂， 生成 Ferric enterobactin ion
  参考文献：
  名称：

  棒杆菌素和丝氨酸三内酯类似物：铁络合物的手性和分子模型。

  摘要：

  由于三价铁离子的水解使其在有氧，接近中性pH的环境中非常不溶，因此大多数细菌会产生铁载体来获取铁（一种基本营养素）。铁铁载体复合物的手性在细胞识别，摄取和利用中起重要作用。从革兰氏阳性细菌中分离出来的棒状杆菌素在结构上与Enterobactin类似，后者首先从革兰氏阴性细菌中分离出来，是众所周知的铁载体，但在三内酯骨架中含有L-苏氨酸而不是L-丝氨酸。棒杆菌素在每个螯合臂中还包含甘氨酸间隔单元。已经制备了具有肠杆菌素的三内酯环和棒杆菌素的甘氨酸间隔基的杂合类似物（丝氨酸-棒杆菌素）。通过分子建模（包括MM3和pBP86 / DN密度泛函理论计算）和圆二色性光谱，研究了肠杆菌素，棒杆菌素和杂合体的三种铁配合物的手性和相对构象稳定性。肠杆菌素形成Delta-铁复​​合物，而棒杆菌素为Lambda。杂合丝氨酸-棒状杆菌素形成近乎外消旋的混合物，而λ-构象异构体稍微过量。每个铁配合物具有四个可能的

  DOI：

  10.1021/ic025531y

文献信息

• Molecular characterization of the Escherichia coli enterobactin cistron entF and coupled expression of entF and the fes gene
  作者：G S Pettis、M A McIntosh

  DOI：10.1128/jb.169.9.4154-4162.1987

  日期：1987.9

  The Escherichia coli entF gene, which encodes the serine-activating enzyme involved in enterobactin synthesis, has been localized to a 4.7-kilobase-pair DNA fragment inserted in the vector pBR328. This recombinant molecule, pITS32, restored the ability of an entF mutant to grow on low-iron medium and to produce enterobactin. Examination of its translation products by minicell and electrophoretic analyses

  大肠杆菌entF基因（编码参与肠杆菌素合成的丝氨酸激活酶）已定位于插入载体pBR328中的4.7碱基对DNA片段。该重组分子pITS32恢复了entF突变体在低铁培养基上生长并产生肠杆菌素的能力。通过微细胞分析和电泳分析对其翻译产物进行检查，发现该蛋白质约为160,000道尔顿，我们将其鉴定为EntF蛋白。当在载体pMC1403中lacZ结构基因上游克隆（pITS301）时，来自pITS32的一个小DNA片段包含entF的翻译起始位点，使得β-半乳糖苷酶的组成型表达较低。相反，克隆（pITS312）包含相同的entF-lacZ融合体和entF上游的较大区域，包括整个fes基因，并延伸到fepA基因（其转录与entF方向相反），以高水平但可诱导的方式表达β-半乳糖苷酶量响应代谢铁浓度的波动。fes基因中的转座子插入突变而非pITS312中fepA 5'区域附近的插入将这种高诱导型表达降低到p
• Brickman T.J.; McIntosh M.A., J Biol Chem, 1992, 0021-9258, 12350-5
  作者：Brickman T.J.、McIntosh M.A.

  DOI：——

  日期：——
• Enterochelin hydrolysis and iron metabolism in Escherichia coli
  作者：I OBRIEN、G COX、F GIBSON

  DOI：10.1016/0304-4165(71)90274-1

  日期：1971.6.22
• A Key Role for the Periplasmic PfeE Esterase in Iron Acquisition <i>via</i> the Siderophore Enterobactin in <i>Pseudomonas aeruginosa</i>
  作者：Quentin Perraud、Lucile Moynié、Véronique Gasser、Mathilde Munier、Julien Godet、Françoise Hoegy、Yves Mély、Gaëtan. L. A. Mislin、James H. Naismith、Isabelle J. Schalk

  DOI：10.1021/acschembio.8b00543

  日期：2018.9.21

  Enterobactin (ENT) is a siderophore (iron-chelating compound) produced by Escherichia coli to gain access to iron, an indispensable nutrient for bacterial growth. ENT is used as an exosiderophore by Pseudomonas aeruginosa with transport of ferri-ENT across the outer membrane by the PfeA transporter. Next to the pfeA gene on the chromosome is localized a gene encoding for an esterase, PfeE, whose transcription is regulated, as for pfeA, by the presence of ENT in bacterial environment. Purified PfeE hydrolyzed ferri-ENT into three molecules of 2,3-DHBS (2,3-dihydroxybenzoylserine) still complexed with ferric iron, and complete dissociation of iron from ENT chelating groups was only possible in the presence of both PfeE and an iron reducer, such as DTT. The crystal structure of PfeE and an inactive PfeE mutant complexed with ferri-ENT or a nonhydrolyzable ferri-catechol complex allowed identification of the enzyme binding site and the catalytic triad. Finally, cell fractionation and fluorescence microscopy showed periplasmic localization of PfeE in P. aeruginosa cells. Thus, the molecular mechanism of iron dissociation from ENT in P. aeruginosa differs from that previously described in E. coli. In P. aeruginosa, siderophore hydrolysis occurs in the periplasm, with ENT never reaching the bacterial cytoplasm. In E. coli, ferri-ENT crosses the inner membrane via the ABC transporter FepBCD and ferri-ENT is hydrolyzed by the esterase Fes only once it is in the cytoplasm.
• HPLC separation of enterobactin and linear 2,3-dihydroxybenzoylserine derivatives: a study on mutants ofEscherichia coli defective in regulation (fur), esterase (fes) and transport (fepA)
  作者：G�nther Winkelmann、Alexander Cansier、Werner Beck、G�nther Jung

  DOI：10.1007/bf00140485

  日期：1994.4

  Reversed-phase HPLC separation of enterobactin and its 2,3-dihydroxybenzoylserine derivatives was used for a comparative analysis of mutants of Escherichia coli, defective in the regulation of enterobactin biosynthesis (fur), enterobactin transport (fepA) and enterobactin esterase (fes). A complete separation of all 2,3-dihydroxybenzoylserine compounds was achieved: the monomer (DHBS), the linear dimer (DHBS)2 and trimer (DHBS)3, the cyclic trimer, enterobactin, as well as 2,3-dihydroxybenzoic acid. The production of all these compounds was followed after ethylacetate extraction from acidified culture fluids. Enterobactin was found to be the predominant product in all mutant strains. The mutant strains behaved differently with regard to the breakdown products. All degradation products, such as DHBS, (DHBS)2 and (DHBS)3, were detected in the overproducing fur mutant where both transport and esterase are still functioning, while only the monomer, DHBS, was detected in the fepA mutant and no degradation was found in the esterase-deficient fes mutant. From the pattern of breakdown products it may be inferred that the esterase acts in two different ways, depending on whether transport is functioning or not. Thus, esterolytic cleavage of ferric enterobactin after entering the cells results in a mixture of all three hydrolysis products, i.e. DHBS, (DHBS)2 and (DHBS)3, while cleavage of iron-free enterobactin subsequent to its biosynthesis yields only the monomer. Thus, the results of quantitative HPLC analysis of enterobactin and its breakdown products show that different enterobactin esterase products arise, depending on whether iron is bound to enterobactin or not.