KEGG   ENZYME: 6.3.2.14Help
Entry
EC 6.3.2.14                 Enzyme                                 

Name
enterobactin synthase;
N-(2,3-dihydroxybenzoyl)-serine synthetase;
2,3-dihydroxybenzoylserine synthetase;
2,3-dihydroxybenzoate---serine ligase
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
2,3-dihydroxybenzoate:L-serine ligase
Reaction(IUBMB)
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate [RN:R07644]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
2,3-dihydroxybenzoate [CPD:C00196];
L-serine [CPD:C00065]
Product
enterobactin [CPD:C05821];
AMP [CPD:C00020];
diphosphate [CPD:C00013]
Comment
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).
History
EC 6.3.2.14 created 1972, modified 2012
Reference
1  [PMID:4966114]
  Authors
Brot N, Goodwin J.
  Title
Regulation of 2,3-dihydroxybenzoylserine synthetase by iron.
  Journal
J. Biol. Chem. 243 (1968) 510-3.
  Organism
Escherichia coli [GN:eco]
Reference
2  [PMID:2531000]
  Authors
Rusnak F, Faraci WS, Walsh CT.
  Title
Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product.
  Journal
Biochemistry. 28 (1989) 6827-35.
Reference
3  [PMID:2139796]
  Authors
Rusnak F, Liu J, Quinn N, Berchtold GA, Walsh CT
  Title
Subcloning of the enterobactin biosynthetic gene entB: expression, purification,  characterization, and substrate specificity of isochorismatase.
  Journal
Biochemistry. 29 (1990) 1425-35.
Reference
4  [PMID:1826089]
  Authors
Rusnak F, Sakaitani M, Drueckhammer D, Reichert J, Walsh CT
  Title
Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine.
  Journal
Biochemistry. 30 (1991) 2916-27.
  Organism
Escherichia coli [GN:eco]
Reference
5  [PMID:9485415]
  Authors
Gehring AM, Mori I, Walsh CT.
  Title
Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF.
  Journal
Biochemistry. 37 (1998) 2648-59.
  Organism
Escherichia coli [GN:eco]
Reference
6  [PMID:10375542]
  Authors
Shaw-Reid CA, Kelleher NL, Losey HC, Gehring AM, Berg C, Walsh CT
  Title
Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization.
  Journal
Chem. Biol. 6 (1999) 385-400.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37318-63-1

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