Information on EC - enterobactin synthase

for references in articles please use BRENDA:EC6.3.2.14
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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
       enterobactin synthase
IUBMB Comments
This enzyme complex catalyses the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyses the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyses the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3-dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule).
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The enzyme appears in viruses and cellular organisms
2,3-Dihydroxy-N-benzoyl-L-serine synthetase, 2,3-Dihydroxybenzoylserine synthetase, DBS synthetase, DHBS synthase, EntE, N-(2,3-Dihydroxybenzoyl)-serine synthetase, Synthetase, 2,3-dihydroxybenzoylserine, more
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate
show the reaction diagram
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