Polyamine oxidase: Difference between revisions
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**[[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]] |
Revision as of 11:24, 13 September 2017
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 13-September-2017