Pyridoxine 5'-phosphate oxidase

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{{STRUCTURE_2aq6| PDB=2aq6 | SIZE=400| SCENE= |right|CAPTION=Pyridoxine 5'-phosphate oxidase dimer complex with pyridoxine 5'-phosphate, [[2aq6]] }}
{{STRUCTURE_2aq6| PDB=2aq6 | SIZE=400| SCENE= |right|CAPTION=Pyridoxine 5'-phosphate oxidase dimer complex with pyridoxine 5'-phosphate, [[2aq6]] }}
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== Function ==
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Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
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'''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, which is a biological essential cofactor. PNPO catalyzes the last step in vitamin B6 metabolism. PNPO uses FMN as cofactor<ref>PMID:12686112</ref>.
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Or use the four-green-boxes-button to insert scrollable text adjacent
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to a Jmol applet. Check out the other buttons as well!
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== Disease ==
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PNPO mutations are present in epilepsy patients<ref>PMID:24645144</ref>.
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'''Pyridoxine 5’-phosphate oxidase''' (PPO) 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, which is a biological essential cofactor. PPO catalyzes the last step in vitamin B6 metabolism. PPO uses FMN as cofactor.
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==3D structures of pyridoxine 5'-phosphate oxidase==
==3D structures of pyridoxine 5'-phosphate oxidase==
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[[1dnl]], [[1g76]], [[1wv4]] – EcPPO – ''Escherichia coli''<br />
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[[1dnl]], [[1g76]], [[1wv4]] – EcPNPO – ''Escherichia coli''<br />
[[1g76]], [[1g77]], [[1g78]], [[1g79]], [[1jnw]] – EcPPO + PLP<br />
[[1g76]], [[1g77]], [[1g78]], [[1g79]], [[1jnw]] – EcPPO + PLP<br />
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[[1nrg]] - hPPO + PLP – human<br />
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[[1nrg]] - hPNPO + PLP – human<br />
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[[3hy8]] - hPPO (mutant) + PLP<br />
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[[3hy8]] - hPNPO (mutant) + PLP<br />
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[[2aq6]] - PPO + PLP – ''Mycobacterium tuberculosis''
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[[2aq6]] - PNPO + PLP – ''Mycobacterium tuberculosis''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:48, 1 August 2016

Template:STRUCTURE 2aq6

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, which 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].

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

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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