Polyamine oxidase

spinqualitylabelsall models lycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), 3l1r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. FAD binding site. Water molecules are shown as red spheres. Spermidine binding site. Whole active site.

3D structures of polyamine oxidase

Updated on 31-May-2026

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• Polyamine oxidase
  • 1yy5, 1rsg, 1xpq – yPAO – yeast
    
  • 3kpf, 4ech, 4gdp – yPAO (mutant)
    
  • 1b37, 1b5q, 1h81 – mPAO FAD-binding domain – maize
• Polyamine oxidase binary complex
  • 1h82, 1h83, 1h84, 1h86 – mPAO FAD-binding domain + polyamine
    
  • 1z6l - yPAO + polyamine
    
  • 3bi2, 3bi4, 3bi5 – yPAO + inhibitor
    
  • 3bnm, 3bnu, 3cnd – yPAO + spermine derivative
    
  • 3cn8, 3cnp, 3cns, 3cnt - yPAO + spermidine derivative
    
  • 3l1r - mPAO (mutant) FAD-binding domain + spermidine
    
  • 3ku9 - mPAO FAD-binding domain (mutant) + spermine
    
• Spermine oxidase or PAO-1
  • 7oxl – hPAO-1 – human
    
  • 7oy0 – hPAO-1 + inhibitor
    

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