Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.

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Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK

Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.

Protein Sci. 2003 Jul;12(7):1455-63. doi: 10.1110/ps.0356203.

PubMed ID

12824491 [ View in PubMed

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Abstract

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 approximately 0.2 sec(-1) and K(m) 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.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Pyridoxine phosphate	Pyridoxine-5'-phosphate oxidase	Protein	Humans	Unknown	Substrate	Details

Polypeptides

Name	UniProt ID
Pyridoxine-5'-phosphate oxidase	Q9NVS9	Details