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- W2915867013 abstract "Abstract Ectoine synthase (EctC) is the signature enzyme for the production of ectoine, a compatible solute and chemical chaperone widely synthesized by bacteria as a cellular defense against the detrimental effects of osmotic stress. EctC catalyzes the last step in ectoine synthesis through cyclo-condensation of the EctA-formed substrate N -gamma-acetyl-L-2,4-diaminobutyric acid via a water elimination reaction. We have biochemically and structurally characterized the EctC enzyme from the thermo-tolerant bacterium Paenibacillus lautus ( Pl ). EctC is a member of the cupin superfamily and forms dimers, both in solution and in crystals. We obtained high-resolution crystal structures of the ( Pl )EctC protein in forms that contain (i) the catalytically important iron, (ii) iron and the substrate N -gamma-acetyl-L-2,4-diaminobutyric acid, and (iii) iron and the enzyme reaction product ectoine. These crystal structures lay the framework for a proposal for the EctC-mediated water-elimination reaction mechanism. Residues involved in coordinating the metal, the substrate, or the product within the active site of ectoine synthase are highly conserved among a large group of EctC-type proteins. Collectively, the biochemical, mutational, and structural data reported here yielded detailed insight into the structure-function relationship of the ( Pl )EctC enzyme and are relevant for a deeper understanding of the ectoine synthase family as a whole." @default.
- W2915867013 created "2019-03-02" @default.
- W2915867013 creator A5002676236 @default.
- W2915867013 creator A5014688926 @default.
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- W2915867013 creator A5047337863 @default.
- W2915867013 creator A5064587433 @default.
- W2915867013 creator A5072628229 @default.
- W2915867013 creator A5073235098 @default.
- W2915867013 creator A5077256764 @default.
- W2915867013 date "2019-01-23" @default.
- W2915867013 modified "2023-10-18" @default.
- W2915867013 title "Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis" @default.
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