Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.

@article{Blickling1997ReactionMO,
  title={Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.},
  author={S Blickling and Christian Renner and Bernd Laber and Hans-Dieter Pohlenz and Tad A. Holak and Robert Huber},
  journal={Biochemistry},
  year={1997},
  volume={36 1},
  pages={
          24-33
        }
}
Dihydrodipicolinate synthase (DHDPS) catalyzes the condensation of pyruvate with L-aspartate beta-semialdehyde. It is the first enzyme unique to the diaminopimelate pathway of lysine biosynthesis. Here we present the crystal structures of five complexes of Escherichia coli DHDPS with substrates, substrate analogs, and inhibitors. These include the complexes of DHDPS with (1) pyruvate, (2) pyruvate and the L-aspartate beta-semialdehyde analog succinate beta-semialdehyde, (3) the inhibitor alpha… 

Figures and Tables from this paper

Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.
TLDR
The crystal structure of DHDPS from Methanocaldococcus jannaschii (MjDHDPS) was solved by the molecular-replacement method and was refined to 2.2 A resolution, revealing that MjD HDPS forms a functional homotetramer, as also observed in Escherichia coli D HDPS, Thermotoga maritima DHDps and Bacillus anthracis DHD PS.
The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.
TLDR
In an attempt to examine the specificity of the active site of DHDPS, the enzyme was cocrystallized with the substrate analogue oxaloacetate andKinetic analysis confirmed that the decarboxylation of oxalo acetate was not catalysed by D HDPS and was instead a slow spontaneous chemical process.
Tetrahydrodipicolinate N-Succinyltransferase and Dihydrodipicolinate Synthase from Pseudomonas aeruginosa: Structure Analysis and Gene Deletion
TLDR
It is shown that tetrahydrodipicolinate N-succinyltransferase (DapD) from P. aeruginosa is specific for the L-stereoisomer of the amino substrate L-2-aminopimelate, and its D-enantiomer acts as a weak inhibitor, indicating that DapA is not an optimal target for drug development against this organism.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate.
TLDR
It is shown that DHDPS from B. anthracis purified in the presence of pyruvate yields greater amounts of recombinant enzyme with more than 20-fold greater specific activity compared with the enzyme purified inThe absence of substrate.
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