Polyamine oxidase: Difference between revisions
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{{STRUCTURE_3l1r| PDB=3l1r | SIZE=400| SCENE= |right|CAPTION=Glycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and | {{STRUCTURE_3l1r| PDB=3l1r | SIZE=400| SCENE= |right|CAPTION=Glycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[3l1r]] }} | ||
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Revision as of 13:42, 30 December 2013
Template:STRUCTURE 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.
3D structures of polyamine oxidase3D structures of polyamine oxidase
1yy5, 1rsg, 1xpq – yPAO – yeast
3kpf – 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