Polyamine oxidase

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{{STRUCTURE_3l1r| PDB=3l1r | SIZE=400| SCENE= |right|CAPTION=Glycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[3l1r]] }}
{{STRUCTURE_3l1r| PDB=3l1r | SIZE=400| SCENE= |right|CAPTION=Glycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[3l1r]] }}
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'''Polyamine oxidase''' (PAO) catalyzes the conversion of N-acetylspermine, molecular oxygen and water to N-acetylspermidine, 3-aminopropanol and hydrogen peroxide. PAO via its production of hydrogen peroxide, is one of the key elements for oxidative burst which induces programmed cell death. PAO is involved in polyamine catabolism and uses FAD as a cofactor<ref>PMID:8584670</ref>.
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'''Polyamine oxidase''' (PAO) catalyzes the conversion of N-acetylspermine, molecular oxygen and water to N-acetylspermidine, 3-aminopropanol and hydrogen peroxide. PAO via its production of hydrogen peroxide, is one of the key elements for oxidative burst which induces programmed cell death. PAO is involved in polyamine catabolism and uses FAD as a cofactor.
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==3D structures of polyamine oxidase==
==3D structures of polyamine oxidase==
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**[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine
**[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:07, 7 July 2016

Template:STRUCTURE 3l1r

Polyamine oxidase (PAO) catalyzes the conversion of N-acetylspermine, molecular oxygen and water to N-acetylspermidine, 3-aminopropanol and hydrogen peroxide. PAO via its production of hydrogen peroxide, is one of the key elements for oxidative burst which induces programmed cell death. PAO is involved in polyamine catabolism and uses FAD as a cofactor[1].

3D structures of polyamine oxidase

Updated on 07-July-2016

References

  1. Seiler N. Polyamine oxidase, properties and functions. Prog Brain Res. 1995;106:333-44. PMID:8584670

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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