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IUBMB CommentsThis 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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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
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-
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ATP + arylated EntB + L-serine
enterobactin + AMP + diphosphate
reaction of EntF
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-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
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
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-
?
ATP + 3-hydroxybenzoate + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
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-
?
ATP + 4-aminosalicylic acid + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
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-
?
ATP + salicylic acid + phosphopantetheinylated EntB
arylated EntB + AMP + diphosphate
reaction of EntE
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-
?
additional information
?
-
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
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-
?
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
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-
?
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
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-
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-
?
ATP + 2,3-dihydroxybenzoate + L-Ser
Products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-Ser
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specific for the substrates
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-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
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-
-
?
ATP + 2,3-dihydroxybenzoate + L-serine
N-(2,3-dihydroxybenzoyl)-L-serine + AMP + diphosphate
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-
-
?
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
?
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-
Ser-dependent ATP-diphosphate exchange
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?
additional information
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no activity with 4-aminobenzoic acid
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?
additional information
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no activity with 4-aminobenzoic acid
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additional information
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no activity with 4-aminobenzoic acid
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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
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-
?
ATP + arylated EntB + L-serine
enterobactin + AMP + diphosphate
reaction of EntF
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-
?
6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine
enterobactin + 6 AMP + 6 diphosphate
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
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-
?
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
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-
?
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
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-
?
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
-
?
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0.0025
2,3-Dihydroxybenzoate
pH 7.8, 25°C, recombinant EntE
0.07
3-hydroxybenzoate
pH 7.8, 25°C, recombinant EntE
3.1
4-aminosalicylic acid
pH 7.8, 25°C, recombinant EntE
0.43
ATP
pH 7.8, 25°C, recombinant EntE
260
L-Ser
-
ATP-diphosphate exchange
0.0029
phosphopantetheinylated EntB
pH 7.8, 25°C, recombinant EntE
-
0.07
salicylic acid
pH 7.8, 25°C, recombinant EntE
additional information
additional information
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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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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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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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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
brenda
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
brenda
Brot, N.; Goodwin, J.
Regulation of 2,3-dihydroxybenzoylserine synthetase by iron
J. Biol. Chem.
243
510-513
1968
Escherichia coli
brenda
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
brenda
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
brenda
Reichert, J.; Sakaitani, M.; Walsh, C.T.
Characterization of EntF as a serine-activating enzyme
Protein Sci.
1
549-556
1992
Escherichia coli
brenda
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
brenda
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
brenda
Sikora, A.L.; Wilson, D.J.; Aldrich, C.C.; Blanchard, J.S.
Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli
Biochemistry
49
3648-3657
2010
Escherichia coli (P0ADI4), Escherichia coli (P10378), Escherichia coli (P11454)
brenda