Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus

@article{Hennig1998CrystalSA,
  title={Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus},
  author={M. J. P. Hennig and Allan D′Arcy and Isabella C. Hampele and Malcolm G.P. Page and Christian Oefner and Glenn E. Dale},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={357-362}
}
Dihydroneopterin aldolase catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin during the de novo synthesis of folk acid from guanosine triphosphate. The gene encoding the dihydroneopterin aldolase from S. aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and its X-ray structure determined at 1.65 Å resolution. The protein forms an octamer of 110,000 M, molecular weight. Four… CONTINUE READING

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