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].
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3D structures of polyamine oxidase3D structures of polyamine oxidase
Updated on 12-August-2019
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- Polyamine oxidase
- 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
ReferencesReferences
- ↑ Seiler N. Polyamine oxidase, properties and functions. Prog Brain Res. 1995;106:333-44. PMID:8584670
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