Enterobactin (also known as enterochelin) is a high affinity siderophore that acquires iron for microbial systems.

[3] Due to its high affinity, enterobactin is capable of chelating even in environments where the concentration of ferric ion is held very low, such as within living organisms.

An amide linkage of DHB to L-serine is then catalyzed by EntD, EntE, EntF and EntB.

[4] Although a number of stereoisomers are possible due to the chirality of the serine residues, only the Δ-cis isomer is metabolically active.

Reduction of the iron (Fe3+ to Fe2+) occurs in conjunction with this cleavage, but no FeEnt bacterial reductase enzyme has been identified, and the mechanism for this process is still unclear.