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 C. Renner and B. Laber and H. Pohlenz and T. Holak and R. 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… Expand
Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.
The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.
Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate.
The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.
...
1
2
3
4
5
...

References

1988)DeVelopment and usage of a molecular graphics
  • 1988