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Information on EC 6.3.2.14 - enterobactin synthase and Organism(s) Escherichia coli and UniProt Accession P0ADI4
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6.3.2.14 enterobactin synthaseIUBMB 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 taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
6
+
3
+
3
=
+
6
+
6
Synonyms
enterobactin synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Dihydroxy-N-benzoyl-L-serine synthetase
-
-
-
-
2,3-Dihydroxybenzoylserine synthetase
-
-
-
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DBS synthetase
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-
-
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DHBS synthase
-
-
-
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EntE
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component of the enterobactin i.e. Tris-(N-(2,3-dihydroxybenzoyl)serine)trilactone, synthetase activity
N-(2,3-Dihydroxybenzoyl)-serine synthetase
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-
-
-
Synthetase, 2,3-dihydroxybenzoylserine
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate
L-Ser-adenylate is an enzyme-bound intermediate
-
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate
bi-uni-uni-bi ping-pong kinetic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide formation
-
-
-
-
carboxamide formation
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
2,3-dihydroxybenzoate:L-serine ligase
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).
CAS REGISTRY NUMBER
COMMENTARY
37318-63-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo)EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
ATP + arylated EntB + L-serine
enterobactin + AMP + diphosphate
reaction of EntF
-
-
?
ATP + 2,3-dihydroxybenzoate + L-Ser
Products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-Ser
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
ATP + 2,3-dihydroxybenzoate + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
-
-
?
ATP + 3-hydroxybenzoate + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
-
-
?
ATP + 4-aminosalicylic acid + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
-
-
?
ATP + salicylic acid + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
-
-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo) EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo)EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
ATP + 2,3-dihydroxybenzoate + L-Ser
Products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-Ser
-
-
-
?
ATP + 2,3-dihydroxybenzoate + L-Ser
Products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-Ser
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-
-
-
?
ATP + 2,3-dihydroxybenzoate + L-Ser
Products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-Ser
-
specific for the substrates
-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
-
-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
-
-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
-
component of enterobactin synthetase activity that specifically transfers the dihydroxybenzoate acyl group onto holo-entB
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
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component of enterobactin synthetase activity that specifically transfers the dihydroxybenzoate acyl group onto holo-entB
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?
additional information
?
-
no activity with 4-aminobenzoic acid
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-
?
additional information
?
-
no activity with 4-aminobenzoic acid
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-
?
additional information
?
-
no activity with 4-aminobenzoic acid
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo)EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
ATP + arylated EntB + L-serine
enterobactin + AMP + diphosphate
reaction of EntF
-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
ATP + 2,3-dihydroxybenzoate + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
-
-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo) EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
overall reaction. EntB, -D, -E, and -F are then required to catalyze the ATP-dependent assembly of enterobactin from three molecules each of 2,3-dihydroxybenzoate and L-serine. EntD, a phosphopantetheinyl transferase, uses coenzyme A to phosphopantetheinylate S245 of the aryl carrier protein domain of EntB. Next, EntE catalyzes the transfer of 2,3-dihydroxybenzoate onto the phosphopantetheinylated (holo)EntB to yield the covalently arylated EntB. Finally, arylated EntB, ATP, and L-serine are used as substrates for the reaction catalyzed by EntF to generate enterobactin
-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
-
component of enterobactin synthetase activity that specifically transfers the dihydroxybenzoate acyl group onto holo-entB
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
-
component of enterobactin synthetase activity that specifically transfers the dihydroxybenzoate acyl group onto holo-entB
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
2,3-Dihydroxybenzoate
pH 7.8, 25°C, recombinant EntE
3.1
4-aminosalicylic acid
pH 7.8, 25°C, recombinant EntE
0.0029
phosphopantetheinylated EntB
pH 7.8, 25°C, recombinant EntE
-
additional information
additional information
two possible kinetic mechanisms can explain nonlinear kinetics: one-step slow association and two-step isomerization, bi-uni-uni-bi ping-pong kinetic mechanism, kinetic analysis, overview
-
additional information
additional information
two possible kinetic mechanisms can explain nonlinear kinetics: one-step slow association and two-step isomerization, bi-uni-uni-bi ping-pong kinetic mechanism, kinetic analysis, overview
-
additional information
additional information
two possible kinetic mechanisms can explain nonlinear kinetics: one-step slow association and two-step isomerization, bi-uni-uni-bi ping-pong kinetic mechanism, kinetic analysis, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
2,3-Dihydroxybenzoate
pH 7.8, 25°C, recombinant EntE
4.4
4-aminosalicylic acid
pH 7.8, 25°C, recombinant EntE
2.8
phosphopantetheinylated EntB
pH 7.8, 25°C, recombinant EntE
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
880
2,3-Dihydroxybenzoate
pH 7.8, 25°C, recombinant EntE
15
4-aminosalicylic acid
pH 7.8, 25°C, recombinant EntE
980
phosphopantetheinylated EntB
pH 7.8, 25°C, recombinant EntE
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
thermodynamics and inhibition kinetics, stopped-flow measurements
-
additional information
additional information
thermodynamics and inhibition kinetics, stopped-flow measurements
-
additional information
additional information
thermodynamics and inhibition kinetics, stopped-flow measurements
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
chorismate is converted to 2,3-dihydroxybenzoate via the sequential catalytic activities of EntC, -B, and -A
metabolism
chorismate is converted to 2,3-dihydroxybenzoate via the sequential catalytic activities of EntC, -B, and -A
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged EntE from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene entE, expression in Escherichia coli strain BL21(DE3)
gene entE, expression in Escherichia coli strain BL21(DE3)
gene entE, expression of His-tagged EntE in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bryce, G.F.; Weller, R.; Brot, N.
Studies on the enzymatic synthesis of 2,3-dihydroxy-N-benzoyl-L-serine in Escherichia coli
Biochem. Biophys. Res. Commun.
42
871-879
1971
Escherichia coli
Bryce, G.F.; Brot, N.
Iron transport in Escherichia coli and its relation to the repression of 2,3-dihydroxy-N-benzoyl-L-serine synthetase
Arch. Biochem. Biophys.
142
399-406
1971
Escherichia coli
Brot, N.; Goodwin, J.
Regulation of 2,3-dihydroxybenzoylserine synthetase by iron
J. Biol. Chem.
243
510-513
1968
Escherichia coli
Brot, N.; Goodwin, J.; Fales, H.
In vivo and in vitro formation of 2,3-dihydroxybenzoylserine by Escherichia coli K12
Biochem. Biophys. Res. Commun.
25
454-461
1966
Escherichia coli, Escherichia coli 2276
McCray, J.W.; Herrmann, K.M.
Derepression of certain aromatic amino acid biosynthetic enzymes of Escherichia coli K-12 by growth in Fe3+-deficient medium
J. Bacteriol.
125
608-615
1976
Escherichia coli
Reichert, J.; Sakaitani, M.; Walsh, C.T.
Characterization of EntF as a serine-activating enzyme
Protein Sci.
1
549-556
1992
Escherichia coli
Gehring, A.M.; Mori, I.; Walsh, C.T.
Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
Biochemistry
37
2648-2659
1998
Escherichia coli
Ehmann, D.E.; Shaw-Reid, C.A.; Losey, H.C.; Walsh, C.T.
The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates
Proc. Natl. Acad. Sci. USA
97
2509-2514
2000
Escherichia coli
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