Polyamine oxidase: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
<StructureSection load='3l1r' size='400' side='right' scene='1m10/Surface/2' 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>. | ||
</StructureSection> | |||
==3D structures of polyamine oxidase== | ==3D structures of polyamine oxidase== | ||
Revision as of 15:06, 7 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]. |
|
3D structures of polyamine oxidase3D structures of polyamine oxidase
Updated on 07-September-2017