Polyamine oxidase: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(6 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<StructureSection load='3l1r' size='400' side='right' scene='1m10/Surface/2' caption='lycosylated FAD containing polyamine oxidase dimer complex  with spermidine, sulfate and Cl- ion (green), [[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]]' >  




'''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>.
*<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>
</StructureSection>
==3D structures of polyamine oxidase==
==3D structures of polyamine oxidase==
Line 22: Line 25:
**[[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 ==
<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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman