Polyamine oxidase: Difference between revisions
No edit summary |
No edit summary |
||
(One intermediate revision by one other user not shown) | |||
Line 1: | Line 1: | ||
<StructureSection load='' size=' | <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>. | '''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/ | *<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/5'>Spermidine binding site</scene>. | ||
*<scene name='48/486448/Cv/6'>Whole active site</scene>. | *<scene name='48/486448/Cv/6'>Whole active site</scene>. |