NADH peroxidase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='450' side='right' scene='48/486476/Cv/1' caption='NADH peroxidase containing FAD complex with NAD, [[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 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. | '''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. | ||
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/13'>NAD binding site</scene>. Water molrcules are shown as red spheres. |
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/14'>NAD/FAD interactions</scene>. |
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/15'>FAD binding site</scene>. |
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/16'>Whole binding site</scene>. |
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/17'>NAD binding pocket</scene>. |
| - | *<scene name='48/486476/Cv/ | + | *<scene name='48/486476/Cv/18'>FAD binding pocket</scene>. |
</StructureSection> | </StructureSection> | ||
==3D structures of NADH peroxidase== | ==3D structures of NADH peroxidase== | ||
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3D structures of NADH peroxidase
1npx, 1joa – EfNPO – Enterococcus faecalis
2npx – EfNPO + NAD
1nhp, 1nhq, 1nhr, 1nhs, 1f8w – EfNPO (mutant)
References
- ↑ 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
