• DOI:10.1021/BI962272D
Corpus ID: 23072673

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
        }
}

• S. Blickling, C. Renner, +3 authors R. Huber
• Published 1997
• Chemistry, Medicine
• Biochemistry

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