Polyamine oxidase

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

Updated on 23-September-2014

1yy5, 1rsg, 1xpq – yPAO – yeast
3kpf, 4ech, 4gdp – yPAO (mutant)
1b37, 1b5q, 1h81 – mPAO FAD-binding domain – maize

Polyamine oxidase binary complexPolyamine 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

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

Michal Harel, Alexander Berchansky, Joel L. Sussman