X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution.

@article{Safo2000XraySO,
  title={X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution.},
  author={Martin K Safo and Irimpan I Mathews and Faik N. Musayev and Martino Luigi di Salvo and Daniel J. Thiel and Donald J. Abraham and Verne Schirch},
  journal={Structure},
  year={2000},
  volume={8 7},
  pages={751-62}
}
BACKGROUND Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high… CONTINUE READING