PMID:1338974

Citation	Reichert, J, Sakaitani, M and Walsh, CT (1992) Characterization of EntF as a serine-activating enzyme. Protein Sci. 1:549-56
Abstract	EntF is the enzyme responsible for serine activation during the biosynthesis of enterobactin (a cyclic trimer of N-dihydroxybenzoyl serine) in Escherichia coli. EntF has been overexpressed and purified to > 90% homogeneity. The enzyme has been shown to complement the entF- MK1 strain in the synthesis of 2,3-dihydroxybenzoyl serine derivatives and exhibits L-serine-dependent ATP[32P] pyrophosphate exchange activity with a Km for serine of 260 mM and a turnover number of 760 min-1. Release of PPi during incubation of EntF with serine and ATP was observed, but with a low turnover number of 1.0 min-1. These results suggested the presence of an enzyme-bound intermediate, which has been shown by gel filtration analysis to be (L-serine)adenylate.
Links	PubMed PMC2142219 Online version:10.1002/pro.5560010410
Keywords	Adenosine Triphosphate/metabolism; Base Sequence; Cloning, Molecular; Diphosphates/metabolism; Enterobactin/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Peptide Synthases/genetics; Peptide Synthases/isolation & purification; Peptide Synthases/metabolism; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Serine/analogs & derivatives; Serine/metabolism
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