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from Escherichia coli, ≥98% (HPLC)

Empirical Formula (Hill Notation):
CAS Number:
Molecular Weight:

biological source

Escherichia coli

Quality Level


≥98% (HPLC)

shipped in

wet ice

storage temp.




InChI key


General description

Enterobactin synthesis occurs via nonribosomal peptide synthetases. The precursor chorismic acid is converted to intermediates isochorismate, 2,3-dihydro-2,3-dihydroxybenzoate and 2,3-dihydroxybenzoic acid (DHB). Final step involves the DHB and L-serine amide linkage. A total of six enzymes (ent A −F) mediate enterobactin biosynthesis.


Enterobactin has been used:
  • as a positive control in tryptophan fluorescence quenching experiments
  • as a reference standard in high performance liquid chromatography to quantify Kosakonia radicincitans culture medium siderophores
  • in the crystallization reservoir to remove iron contamination in the medium and in Fe-enterbactin binding studies

This preparation of enterobactin is not bound to iron and will bind to Fe3+ and Fe2+ in solution.

Biochem/physiol Actions

Iron mobilization and uptake by microbes is mediated by low molecular weight complexing agents named siderophores. Enterobactin is a catechol (a benzenediol, C6H4(OH)2) type siderophore produced in small quantities by Escherichia coli and related enteric bacteria when grown on iron deficient media, and is one of the most powerful ferric ion complexing agents known. Enterobactin is a very effective sequestering agent for iron, able to remove iron from proteins, insoluble iron complexes, and other siderophores. Studies of the chemistry, regulation, synthesis, recognition, and transport of enterobactin make it the best-understood siderophore.

Storage Class Code

11 - Combustible Solids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

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Certificate of Origin

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Quotes and Ordering

Shubhangi Agarwal et al.
Scientific reports, 7, 42812-42812 (2017-02-22)
Molecular mechanisms of xenosiderophore and heme acquisitions using periplasmic binding protein (PBP) dependent ATP-binding cassette transporters to scavenge the essential nutrient iron are elusive yet in Vibrio cholerae. Our current study delineates the structures, dynamics and ligand binding properties of
Neal Paragas et al.
Biochimica et biophysica acta, 1823(9), 1451-1458 (2012-06-26)
Kidney damage induces the expression of a myriad of proteins in the serum and in the urine. The function of these proteins in the sequence of damage and repair is now being studied in genetic models and by novel imaging
Agustín Estrada-Peña et al.
Pathogens (Basel, Switzerland), 9(4) (2020-04-26)
Ixodes scapularis ticks harbor microbial communities including pathogenic and non-pathogenic microbes. Pathogen infection increases the expression of several tick gut proteins, which disturb the tick gut microbiota and impact bacterial biofilm formation. Anaplasma phagocytophilum induces ticks to express I. scapularis
Pyoverdine, the major siderophore in Pseudomonas aeruginosa, evades NGAL recognition
Peek ME, et al.
Interdisciplinary perspectives on infectious diseases, 2012 (2012)
L M Bogomolnaya et al.
mBio, 11(3) (2020-05-07)
Nontyphoidal salmonellae (NTS) are exposed to reactive oxygen species (ROS) during their residency in the gut. To survive oxidative stress encountered during infection, salmonellae employ several mechanisms. One of these mechanisms involves the multidrug efflux pump MacAB, although the natural

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