Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
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DOI:
10.1021/bi970453p
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发表时间:
1997-07-15
期刊:
影响因子:
2.9
通讯作者:
Walsh, CT
中科院分区:
文献类型:
--
作者:
Gehring, AM;Bradley, KA;Walsh, CT
In Escherichin coli, the siderophore molecule enterobactin is synthesized in response to iron deprivation by formation of an amide bond between 2,3-dihydroxybenzoate (2,3-DHB) and L-serine and formation of eater linkages between three such N-acylated serine residues, We show that EntB, previously described as the isochorismate lyase required for production of 2,3-DHB, is a bifunctional protein that also serves as an aryl carrier protein (ArCP) with a role in enterobactin assembly, EntB is phosphopantetheinylated near the C terminus in a reaction catalyzed by EntD with a k(cat) of 5 min(-1) and a K-m for apo-EntB of 6.5 mu M. This holo-EntB is then acylated with 2,3-DHB in a reaction catalyzed by EntE, previously described as the 2,3-DHB-AMP ligase, with a k(cat) of 100 min(-1) and a k(m) of