NADH peroxidase

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{{STRUCTURE_2npx| PDB=2npx | SIZE=350| SCENE= |right|CAPTION=NADH peroxidase containing FAD complex with NAD, [[2npx]] }}
{{STRUCTURE_2npx| PDB=2npx | SIZE=350| SCENE= |right|CAPTION=NADH peroxidase containing FAD complex with NAD, [[2npx]] }}
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'''NADH peroxidase''' (NPO) catalyzes the conversion of NADH to NAD+ using hydrogen peroxide. See [[NAD]]. NPO eliminates the potentially toxic hydrogen peroxide and defends the cell against H<sub>2</sub>O<sub>2</sub>-mediated oxidative stress<ref>PMID:8425532</ref>. NPO provides an additional pathway for regeneration of NAD+ which is essential to the fermentative metabolism. FAD is the cofactor in this reaction.
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'''NADH peroxidase''' (NPO) catalyzes the conversion of NADH to NAD+ using hydrogen peroxide. See [[NAD]]. NPO eliminates the potentially toxic hydrogen peroxide and defends the cell against H2O2-mediated oxidative stress. NPO provides an additional pathway for regeneration of NAD+ which is essential to the fermentative metabolism. FAD is the cofactor in this reaction.
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==3D structures of NADH peroxidase==
==3D structures of NADH peroxidase==
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[[2npx]] – EfNPO + NAD<br />
[[2npx]] – EfNPO + NAD<br />
[[1nhp]], [[1nhq]], [[1nhr]], [[1nhs]], [[1f8w]] – EfNPO (mutant)
[[1nhp]], [[1nhq]], [[1nhr]], [[1nhs]], [[1f8w]] – EfNPO (mutant)
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== References ==
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<references/>

Revision as of 08:40, 5 May 2016

Template:STRUCTURE 2npx


NADH peroxidase (NPO) catalyzes the conversion of NADH to NAD+ using hydrogen peroxide. See NAD. NPO eliminates the potentially toxic hydrogen peroxide and defends the cell against H2O2-mediated oxidative stress[1]. NPO provides an additional pathway for regeneration of NAD+ which is essential to the fermentative metabolism. FAD is the cofactor in this reaction.

3D structures of NADH peroxidase

1npx, 1joa – EfNPO – Enterococcus faecalis
2npx – EfNPO + NAD
1nhp, 1nhq, 1nhr, 1nhs, 1f8w – EfNPO (mutant)

References

  1. ↑ Stehle T, Claiborne A, Schulz GE. NADH binding site and catalysis of NADH peroxidase. Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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