Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB).

@article{Girish2011StructureAN,
  title={Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB).},
  author={Tavarekere S. Girish and Vikas Navratna and Balasubramanian Gopal},
  journal={FEBS letters},
  year={2011},
  volume={585 16},
  pages={2561-7}
}
Lysine biosynthesis proceeds by the nucleotide-dependent reduction of dihydrodipicolinate (DHDP) to tetrahydrodipicolinate (THDP) by dihydrodipicolinate reductase (DHDPR). The S. aureus DHDPR structure reveals different conformational states of this enzyme even in the absence of a substrate or nucleotide-cofactor. Despite lacking a conserved basic residue essential for NADPH interaction, S. aureus DHDPR differs from other homologues as NADPH is a more preferred co-factor than NADH. The… CONTINUE READING