Skip to main content
Article thumbnail
Location of Repository

Structure and properties of recombinant human pyridoxine 5′-phosphate oxidase

By Faik N. Musayev, Martino L. Di Salvo, Tzu-Ping Ko, Verne Schirch and Martin K. Safo


Pyridoxine 5′-phosphate oxidase catalyzes the terminal step in the synthesis of pyridoxal 5′-phosphate. The cDNA for the human enzyme has been cloned and expressed in Escherichia coli. The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of ∼0.2 sec−1 and Km values in the low micromolar range for both pyridoxine 5′phosphate and pyridoxamine 5′-phosphate. Pyridoxal 5′-phosphate is an effective product inhibitor. The three-dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes. The human and E. coli enzymes share 39% sequence identity, but the binding sites for the tightly bound FMN and substrate are highly conserved. As observed with the E. coli enzyme, the human enzyme binds one molecule of pyridoxal 5′-phosphate tightly on each subunit

Topics: Article
Publisher: Cold Spring Harbor Laboratory Press
OAI identifier:
Provided by: PubMed Central
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://www.pubmedcentral.nih.g... (external link)
  • Suggested articles

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.