Polyamine oxidase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='48/486448/Cv/1' caption='lycosylated FAD containing polyamine oxidase dimer complex with spermidine, sulfate and Cl- ion (green), [[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<ref>PMID:8584670</ref>. | |||
*<scene name='48/486448/Cv/7'>FAD binding site</scene>. Water molecules are shown as red spheres. | |||
*<scene name='48/486448/Cv/5'>Spermidine binding site</scene>. | |||
*<scene name='48/486448/Cv/6'>Whole active site</scene>. | |||
</StructureSection> | |||
==3D structures of polyamine oxidase== | ==3D structures of polyamine oxidase== | ||
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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/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||