Polyamine oxidase

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<StructureSection load='3l1r' size='400' side='right' scene='48/486448/Cv/1' caption='lycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[3l1r]]' >
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<StructureSection load='' size='350' side='right' scene='48/486448/Cv/1' caption='lycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[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<ref>PMID:8584670</ref>.
'''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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*<scene name='48/486448/Cv/4'>FAD binding site</scene>. Water molecules shown as red spheres.
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*<scene name='48/486448/Cv/7'>FAD binding site</scene>. Water molecules are shown as red spheres.
*<scene name='48/486448/Cv/5'>Spermidine binding site</scene>.
*<scene name='48/486448/Cv/5'>Spermidine binding site</scene>.
*<scene name='48/486448/Cv/6'>Whole active site</scene>.
*<scene name='48/486448/Cv/6'>Whole active site</scene>.
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**[[3bnm]], [[3bnu]], [[3cnd]] – yPAO + spermine derivative<br />
**[[3bnm]], [[3bnu]], [[3cnd]] – yPAO + spermine derivative<br />
**[[3cn8]], [[3cnp]], [[3cns]], [[3cnt]] - yPAO + spermidine derivative<br />
**[[3cn8]], [[3cnp]], [[3cns]], [[3cnt]] - yPAO + spermidine derivative<br />
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**[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine
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**[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine<br />
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**[[3ku9]] - mPAO FAD-binding domain (mutant) + spermine<br />
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}}
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== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

lycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), 3l1r

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3D structures of polyamine oxidase

Updated on 12-August-2019

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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