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Gene Review:

ECs0634 - 2,3-dihydro-2,3-dihydroxybenzoate synthetase

Escherichia coli O157:H7 str. Sakai

Gehring, A.M. et al., Drake, E.J. et al.

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Disease relevance of ECs0634

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 [1].

High impact information on ECs0634

We present here the crystal structure of the EntB protein that contains an N-terminal isochorismate lyase domain that functions in the synthesis of 2,3-dihydroxybenzoate and a C-terminal carrier protein domain [2].
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 [1].

References

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. Gehring, A.M., Bradley, K.A., Walsh, C.T. Biochemistry (1997) [Pubmed]
Structure of the EntB Multidomain Nonribosomal Peptide Synthetase and Functional Analysis of Its Interaction with the EntE Adenylation Domain. Drake, E.J., Nicolai, D.A., Gulick, A.M. Chem. Biol. (2006) [Pubmed]

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