Pyridoxamine 5’-phosphate oxidase (PNPO) is an enzyme that plays a crucial role in the metabolism of vitamin B6. It is responsible for the conversion of pyridoxamine 5’-phosphate (PMP) and pyridoxine 5’-phosphate (PNP) to pyridoxal 5’-phosphate (PLP), the active form of vitamin B6. This enzyme is essential for various biological processes, including amino acid metabolism, neurotransmitter synthesis, and gene expression regulation.
PNPO is a flavoprotein that requires flavin mononucleotide (FMN) as a cofactor for its enzymatic activity. The enzyme is encoded by the PNPO gene, which is located on chromosome 17 in humans. The PNPO protein consists of 261 amino acids and has a molecular weight of approximately 30 kDa .
The enzyme catalyzes the oxidation of PMP and PNP to PLP through a two-step reaction. In the first step, PMP or PNP is oxidized to pyridoxal 5’-phosphate (PLP) and hydrogen peroxide (H2O2). In the second step, the hydrogen peroxide is reduced to water, completing the reaction cycle .
PLP, the product of the PNPO-catalyzed reaction, is a vital coenzyme involved in numerous enzymatic reactions. It participates in the metabolism of amino acids, the synthesis of neurotransmitters such as serotonin, dopamine, and gamma-aminobutyric acid (GABA), and the regulation of gene expression. PLP deficiency can lead to various health issues, including neurological disorders, anemia, and impaired immune function .
Mouse anti-human PNPO antibodies are valuable tools in various research applications, including: