Polyamine oxidase: Difference between revisions

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{{STRUCTURE_3l1r|  PDB=3l1r  | SIZE=400| SCENE= |right|CAPTION=Yeast polyamine oxidase Fms1 complex  with spermidine, sulfate and chloride ion, [[3l1r]] }}
<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]]' >  
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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.


'''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>.
*<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/6'>Whole active site</scene>.
</StructureSection>
==3D structures of polyamine oxidase==
==3D structures of polyamine oxidase==


[[1yy5]], [[1rsg]], [[1xpq]] – yPAO – yeast<br />
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[3kpf]] – yPAO (mutant)<br />
{{#tree:id=OrganizedByTopic|openlevels=0|
[[1b37]], [[1b5q]], [[1h81]] – mPAO FAD-binding domain – maize
 
*Polyamine oxidase
 
**[[1yy5]], [[1rsg]], [[1xpq]] – yPAO – yeast<br />
**[[3kpf]], [[4ech]], [[4gdp]] – yPAO (mutant)<br />
**[[1b37]], [[1b5q]], [[1h81]] – mPAO FAD-binding domain – maize


'''Polyamine oxidase binary complex'''
*Polyamine oxidase binary complex


[[1h82]], [[1h83]], [[1h84]], [[1h86]] – mPAO FAD-binding domain + polyamine<br />
**[[1h82]], [[1h83]], [[1h84]], [[1h86]] – mPAO FAD-binding domain + polyamine<br />
[[1z6l]] - yPAO + polyamine<br />
**[[1z6l]] - yPAO + polyamine<br />
[[3bi2]], [[3bi4]], [[3bi5]] – yPAO + inhibitor<br />
**[[3bi2]], [[3bi4]], [[3bi5]] – yPAO + inhibitor<br />
[[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 />
[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine
**[[3l1r]] - mPAO (mutant) FAD-binding domain + spermidine<br />
**[[3ku9]] - mPAO FAD-binding domain (mutant) + spermine<br />


}}
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 16:26, 12 August 2019


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].

  • . Water molecules are shown as red spheres.
  • .
  • .

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

Drag the structure with the mouse to rotate

3D structures of polyamine oxidase3D structures of polyamine oxidase

Updated on 12-August-2019

ReferencesReferences

  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