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
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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).
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
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
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
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
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
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
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
The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates