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- W2771694326 endingPage "162" @default.
- W2771694326 startingPage "153" @default.
- W2771694326 abstract "Dihydrodipicolinate synthase (DHDPS) is critical to the production of lysine through the diaminopimelate (DAP) pathway. Elucidation of the function, regulation and structure of this key class I aldolase has been the focus of considerable study in recent years, given that the dapA gene encoding DHDPS has been found to be essential to bacteria and plants. Allosteric inhibition by lysine is observed for DHDPS from plants and some bacterial species, the latter requiring a histidine or glutamate at position 56 (Escherichia coli numbering) over a basic amino acid. Structurally, two DHDPS monomers form the active site, which binds pyruvate and (S)-aspartate β-semialdehyde, with most dimers further dimerising to form a tetrameric arrangement around a solvent-filled centre cavity. The architecture and behaviour of these dimer-of-dimers is explored in detail, including biophysical studies utilising analytical ultracentrifugation, small-angle X-ray scattering and macromolecular crystallography that show bacterial DHDPS tetramers adopt a head-to-head quaternary structure, compared to the back-to-back arrangement observed for plant DHDPS enzymes. Finally, the potential role of pyruvate in providing substrate-mediated stabilisation of DHDPS is considered." @default.
- W2771694326 created "2017-12-22" @default.
- W2771694326 creator A5046727597 @default.
- W2771694326 creator A5052222929 @default.
- W2771694326 creator A5052660856 @default.
- W2771694326 creator A5068775841 @default.
- W2771694326 creator A5089976475 @default.
- W2771694326 date "2017-12-05" @default.
- W2771694326 modified "2023-09-26" @default.
- W2771694326 title "Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis" @default.
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