Enterobactin (BioDeep_00000409553)

Main id: BioDeep_00000004282

 

natural product


代谢物信息卡片


Enterobactin

化学式: C30H27N3O15 (669.1442)
中文名称:
谱图信息: 最多检出来源 () 0%

分子结构信息

SMILES: C1C(C(=O)OCC(C(=O)OCC(C(=O)O1)NC(=O)C2=C(C(=CC=C2)O)O)NC(=O)C3=C(C(=CC=C3)O)O)NC(=O)C4=C(C(=CC=C4)O)O
InChI: InChI=1S/C30H27N3O15/c34-19-7-1-4-13(22(19)37)25(40)31-16-10-46-29(44)18(33-27(42)15-6-3-9-21(36)24(15)39)12-48-30(45)17(11-47-28(16)43)32-26(41)14-5-2-8-20(35)23(14)38/h1-9,16-18,34-39H,10-12H2,(H,31,40)(H,32,41)(H,33,42)/t16-,17-,18-/m0/s1

描述信息

A macrotriolide produced by certain members of Enterobacteriaceae, e.g. Escherichia coli and Salmonella.
D064449 - Sequestering Agents > D002614 - Chelating Agents > D007502 - Iron Chelating Agents

同义名列表

2 个代谢物同义名

Enterobactin; Enterochelin



数据库引用编号

14 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(1)

PlantCyc(0)

代谢反应

0 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

COVID-19 Disease Map(0)

PathBank(0)

PharmGKB(0)

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表
Cytoplasm 8 ACO1, ARMC1, BDH2, FES, HELB, IREB2, TGM3, WNT2
Endosome membrane 1 TF
Nucleus 1 HELB
cytosol 7 ACO1, ARMC1, BDH2, EHHADH, FES, HELB, IREB2
nuclear body 1 HELB
nucleoplasm 2 ATP2B1, HELB
Cell membrane 3 ATP2B1, SIT1, SLC22A17
Multi-pass membrane protein 3 ATP2B1, SIT1, SLC22A17
Synapse 1 ATP2B1
cell surface 1 TF
glutamatergic synapse 1 ATP2B1
Golgi apparatus 2 ACO1, FES
mitochondrial inner membrane 1 ATP5ME
presynaptic membrane 1 ATP2B1
Cytoplasm, cytosol 1 ACO1
plasma membrane 5 ATP2B1, FES, SIT1, SLC22A17, TF
synaptic vesicle membrane 1 ATP2B1
Membrane 2 ATP2B1, FES
apical plasma membrane 2 SIT1, TF
basolateral plasma membrane 1 ATP2B1
extracellular exosome 8 ACO1, ATP2B1, BDH2, HP, LCN2, SIT1, TF, TGM3
endoplasmic reticulum 1 ACO1
extracellular space 5 CXCL8, HP, LCN2, TF, WNT2
perinuclear region of cytoplasm 1 TF
mitochondrion 5 ACO1, ARMC1, ATP5ME, HELB, IREB2
protein-containing complex 1 TGM3
intracellular membrane-bounded organelle 1 ATP2B1
Single-pass type I membrane protein 1 SIT1
Secreted 5 CXCL8, HP, LCN2, TF, WNT2
extracellular region 5 CXCL8, HP, LCN2, TF, WNT2
cytoplasmic side of plasma membrane 1 FES
Mitochondrion outer membrane 1 ARMC1
mitochondrial outer membrane 1 ARMC1
basal part of cell 1 TF
Cytoplasmic vesicle lumen 1 LCN2
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane 1 ATP2B1
Secreted, extracellular space, extracellular matrix 1 WNT2
cytoplasmic vesicle 2 FES, TF
microtubule cytoskeleton 1 FES
Wnt signalosome 1 WNT2
Early endosome 1 TF
clathrin-coated pit 1 TF
recycling endosome 1 TF
vesicle 1 TF
Apical cell membrane 1 SIT1
Cytoplasm, cytoskeleton 1 FES
focal adhesion 1 FES
Peroxisome 1 EHHADH
peroxisomal matrix 1 EHHADH
collagen-containing extracellular matrix 1 WNT2
lateral plasma membrane 1 ATP2B1
Late endosome 1 TF
cell projection 1 ATP2B1
Chromosome 1 HELB
cytoskeleton 1 FES
blood microparticle 2 HP, TF
Basolateral cell membrane 1 ATP2B1
organelle membrane 1 SLC22A17
site of double-strand break 1 HELB
Presynaptic cell membrane 1 ATP2B1
basal plasma membrane 1 TF
secretory granule lumen 1 TF
HFE-transferrin receptor complex 1 TF
endoplasmic reticulum lumen 1 TF
specific granule lumen 2 HP, LCN2
tertiary granule lumen 1 HP
endocytic vesicle 1 TF
immunological synapse 1 ATP2B1
clathrin-coated endocytic vesicle membrane 1 TF
extrinsic component of cytoplasmic side of plasma membrane 1 TGM3
proton-transporting ATP synthase complex 1 ATP5ME
vesicle coat 1 TF
endocytic vesicle lumen 1 HP
haptoglobin-hemoglobin complex 1 HP
proton-transporting ATP synthase complex, coupling factor F(o) 1 ATP5ME
vacuolar membrane 1 SLC22A17
photoreceptor ribbon synapse 1 ATP2B1
Vacuole membrane 1 SLC22A17
dense body 1 TF
Cytoplasmic granule lumen 1 LCN2


文献列表

  • Alexandra Canciu, Andreea Cernat, Mihaela Tertis, Silvia Botarca, Madalina Adriana Bordea, Joseph Wang, Cecilia Cristea. Proof of Concept for the Detection with Custom Printed Electrodes of Enterobactin as a Marker of Escherichia coli. International journal of molecular sciences. 2022 Aug; 23(17):. doi: 10.3390/ijms23179884. [PMID: 36077283]
  • Chuchu Guo, Elizabeth M Nolan. Heavy-Metal Trojan Horse: Enterobactin-Directed Delivery of Platinum(IV) Prodrugs to Escherichia coli. Journal of the American Chemical Society. 2022 07; 144(28):12756-12768. doi: 10.1021/jacs.2c03324. [PMID: 35803281]
  • Arwen E Frick-Cheng, Anna Sintsova, Sara N Smith, Ali Pirani, Evan S Snitkin, Harry L T Mobley. Ferric Citrate Uptake Is a Virulence Factor in Uropathogenic Escherichia coli. mBio. 2022 06; 13(3):e0103522. doi: 10.1128/mbio.01035-22. [PMID: 35546538]
  • Ashish Kumar, Taihao Yang, Somnath Chakravorty, Aritri Majumdar, Brittany L Nairn, David A Six, Naara Marcondes Dos Santos, Sarah L Price, Matthew B Lawrenz, Luis A Actis, Marilis Marques, Thomas A Russo, Salete M Newton, Phillip E Klebba. Fluorescent sensors of siderophores produced by bacterial pathogens. The Journal of biological chemistry. 2022 03; 298(3):101651. doi: 10.1016/j.jbc.2022.101651. [PMID: 35101443]
  • Vladimir Gorshkov, Olga Parfirova, Olga Petrova, Natalia Gogoleva, Evgeny Kovtunov, Vladimir Vorob'ev, Yuri Gogolev. The Knockout of Enterobactin-Related Gene in Pectobacterium atrosepticum Results in Reduced Stress Resistance and Virulence towards the Primed Plants. International journal of molecular sciences. 2021 Sep; 22(17):. doi: 10.3390/ijms22179594. [PMID: 34502502]
  • Qihao Wu, Kurt Throckmorton, Mitasree Maity, Marc G Chevrette, Doug R Braun, Scott R Rajski, Cameron R Currie, Michael G Thomas, Tim S Bugni. Bacillibactins E and F from a Marine Sponge-Associated Bacillus sp. Journal of natural products. 2021 01; 84(1):136-141. doi: 10.1021/acs.jnatprod.0c01170. [PMID: 33337146]
  • Ximin Zeng, Huiwen Wang, Canghai Huang, Catherine M Logue, Nicolle L Barbieri, Lisa K Nolan, Jun Lin. Evaluation of the Immunogenic Response of a Novel Enterobactin Conjugate Vaccine in Chickens for the Production of Enterobactin-Specific Egg Yolk Antibodies. Frontiers in immunology. 2021; 12(?):629480. doi: 10.3389/fimmu.2021.629480. [PMID: 33868248]
  • Piu Saha, Beng San Yeoh, Xia Xiao, Rachel M Golonka, Ahmed A Abokor, Camilla F Wenceslau, Yatrik M Shah, Bina Joe, Matam Vijay-Kumar. Enterobactin induces the chemokine, interleukin-8, from intestinal epithelia by chelating intracellular iron. Gut microbes. 2020 11; 12(1):1-18. doi: 10.1080/19490976.2020.1841548. [PMID: 33171063]
  • Hari Parapatla, Ramurthy Gudla, Guruprasad Varma Konduru, Elsin Raju Devadasu, Hampapathula Adimurthy Nagarajaram, Manjula Sritharan, Rajagopal Subramanyam, Dayananda Siddavattam. Organophosphate hydrolase interacts with ferric-enterobactin and promotes iron uptake in association with TonB-dependent transport system. The Biochemical journal. 2020 08; 477(15):2821-2840. doi: 10.1042/bcj20200299. [PMID: 32686828]
  • Clémence Massip, Camille V Chagneau, Michèle Boury, Eric Oswald. The synergistic triad between microcin, colibactin, and salmochelin gene clusters in uropathogenic Escherichia coli. Microbes and infection. 2020 04; 22(3):144-147. doi: 10.1016/j.micinf.2020.01.001. [PMID: 31954842]
  • Edyta Konecka, Joanna Mokracka, Sylwia Krzymińska, Adam Kaznowski. Evaluation of The Pathogenic Potential of Insecticidal Serratia marcescens Strains to Humans. Polish journal of microbiology. 2019; 68(2):185-191. doi: 10.21307/pjm-2019-018. [PMID: 31257791]
  • Jérémy Esque, Mark S P Sansom, Marc Baaden, Christophe Oguey. Analyzing protein topology based on Laguerre tessellation of a pore-traversing water network. Scientific reports. 2018 09; 8(1):13540. doi: 10.1038/s41598-018-31422-5. [PMID: 30202114]
  • M Moreno, A Zacarias, A Porzel, L Velasquez, G Gonzalez, M Alegría-Arcos, F Gonzalez-Nilo, E K U Gross. IR and NMR spectroscopic correlation of enterobactin by DFT. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 2018 Jun; 198(?):264-277. doi: 10.1016/j.saa.2018.02.060. [PMID: 29550657]
  • Akira Ishii, Goro Katsuura, Hirotaka Imamaki, Hiroyuki Kimura, Keita P Mori, Takashige Kuwabara, Masato Kasahara, Hideki Yokoi, Kousaku Ohinata, Tomoko Kawanishi, Junichi Tsuchida, Yuji Nakamoto, Kazuwa Nakao, Motoko Yanagita, Masashi Mukoyama, Kiyoshi Mori. Obesity-promoting and anti-thermogenic effects of neutrophil gelatinase-associated lipocalin in mice. Scientific reports. 2017 Nov; 7(1):15501. doi: 10.1038/s41598-017-15825-4. [PMID: 29138470]
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  • Thomas A Russo, Ruth Olson, Ulrike MacDonald, Janet Beanan, Bruce A Davidson. Aerobactin, but not yersiniabactin, salmochelin, or enterobactin, enables the growth/survival of hypervirulent (hypermucoviscous) Klebsiella pneumoniae ex vivo and in vivo. Infection and immunity. 2015 Aug; 83(8):3325-33. doi: 10.1128/iai.00430-15. [PMID: 26056379]
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  • Timothée J N Kenla, Michel D Kongue Tatong, Ferdinand Mouafo Talontsi, Birger Dittrich, Holm Frauendorf, Hartmut Laatsch. Si-enterobactin from the endophytic Streptomyces sp. KT-S1-B5--a potential silicon transporter in Nature?. Chemical communications (Cambridge, England). 2013 Sep; 49(69):7641-3. doi: 10.1039/c3cc44437f. [PMID: 23872808]
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  • Sierra L Hartney, Sylvie Mazurier, Teresa A Kidarsa, Maria Carolina Quecine, Philippe Lemanceau, Joyce E Loper. TonB-dependent outer-membrane proteins and siderophore utilization in Pseudomonas fluorescens Pf-5. Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine. 2011 Apr; 24(2):193-213. doi: 10.1007/s10534-010-9385-2. [PMID: 21080032]
  • Jian Wang, Kostas Pantopoulos. Regulation of cellular iron metabolism. The Biochemical journal. 2011 Mar; 434(3):365-81. doi: 10.1042/bj20101825. [PMID: 21348856]
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  • Surendranathan Devanathan, Kathleen Postle. Studies on colicin B translocation: FepA is gated by TonB. Molecular microbiology. 2007 Jul; 65(2):441-53. doi: 10.1111/j.1365-2958.2007.05808.x. [PMID: 17578453]
  • Friederike Feldmann, Liisa Johanna Sorsa, Kirsten Hildinger, Sören Schubert. The salmochelin siderophore receptor IroN contributes to invasion of urothelial cells by extraintestinal pathogenic Escherichia coli in vitro. Infection and immunity. 2007 Jun; 75(6):3183-7. doi: 10.1128/iai.00656-06. [PMID: 17353289]
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