Pyridoxine 5'-phosphate oxidase
From Proteopedia
Contents |
Function
Pyridoxine 5’-phosphate oxidase (PNPO) catalyzes the oxidation of pyridoxamine-phosphate by molecular oxygen producing pyridoxal 5’-phosphate, ammonia and hydrogen peroxide. Pyridoxal 5’-phosphate (PLP), commonly known as vitamin B6, is a biological essential cofactor. PNPO catalyzes the last step in vitamin B6 metabolism. PNPO uses FMN as cofactor[1].
Disease
PNPO mutations are present in epilepsy patients[2].
Structural highlights
The active site of PNPO shows the product of PNPO catalysis - PLP - interacting with both subunits of the enzyme[3].
3D structures of pyridoxine 5'-phosphate oxidase
1dnl, 1g76, 1wv4 – EcPNPO – Escherichia coli
1g76, 1g77, 1g78, 1g79, 1jnw – EcPPO + PLP
1nrg - hPNPO + PLP – human
3hy8 - hPNPO (mutant) + PLP
2aq6 - PNPO + PLP – Mycobacterium tuberculosis
References
- ↑ di Salvo ML, Safo MK, Musayev FN, Bossa F, Schirch V. Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):76-82. PMID:12686112
- ↑ Mills PB, Camuzeaux SS, Footitt EJ, Mills KA, Gissen P, Fisher L, Das KB, Varadkar SM, Zuberi S, McWilliam R, Stodberg T, Plecko B, Baumgartner MR, Maier O, Calvert S, Riney K, Wolf NI, Livingston JH, Bala P, Morel CF, Feillet F, Raimondi F, Del Giudice E, Chong WK, Pitt M, Clayton PT. Epilepsy due to PNPO mutations: genotype, environment and treatment affect presentation and outcome. Brain. 2014 May;137(Pt 5):1350-60. doi: 10.1093/brain/awu051. Epub 2014 Mar 18. PMID:24645144 doi:http://dx.doi.org/10.1093/brain/awu051
- ↑ Biswal BK, Cherney MM, Wang M, Garen C, James MN. Structures of Mycobacterium tuberculosispyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1492-9. Epub 2005, Oct 19. PMID:16239726 doi:10.1107/S0907444905026673
