User:Eduarda Franco Marcolino/Sandbox 2
From Proteopedia
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==Peroxiredoxin 3 (Prx3), Human== | ==Peroxiredoxin 3 (Prx3), Human== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page '''Eduarda Franco Marcolino/Sandbox 2'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
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| - | ==Introduction== | ||
Peroxiredoxin 3 (Prx3) is a crucial antioxidant enzyme primarily found in the mitochondria, where it plays a vital role in protecting cells from oxidative stress. It belongs to the 2-Cys peroxiredoxin family, characterized by two key cysteine residues essential for its function. Prx3 reduces harmful hydrogen peroxide (H₂O₂) and organic hydroperoxides to water and alcohol, respectively, thereby maintaining cellular redox balance and influencing processes like apoptosis. Its unique mitochondrial localization makes it a key player in managing reactive oxygen species (ROS) produced during cellular respiration. | Peroxiredoxin 3 (Prx3) is a crucial antioxidant enzyme primarily found in the mitochondria, where it plays a vital role in protecting cells from oxidative stress. It belongs to the 2-Cys peroxiredoxin family, characterized by two key cysteine residues essential for its function. Prx3 reduces harmful hydrogen peroxide (H₂O₂) and organic hydroperoxides to water and alcohol, respectively, thereby maintaining cellular redox balance and influencing processes like apoptosis. Its unique mitochondrial localization makes it a key player in managing reactive oxygen species (ROS) produced during cellular respiration. | ||
| - | + | <StructureSection load='5ucx' size='340' side='right' caption='Caption for this structure' scene=''> | |
== Function == | == Function == | ||
| + | Prx3 operates through a redox cycle involving two critical cysteine residues: a peroxidatic cysteine (Cys47) and a resolving cysteine (Cys168). Cys47 reacts with peroxides, forming sulfenic acid, which then reacts with Cys168 to form an intersubunit disulfide bond within a dimer. This disulfide bond is subsequently reduced by the thioredoxin system. (thioredoxin and thioredoxin reductase), regenerating the enzyme for further catalysis. High levels of H₂O₂ can lead to overoxidation and inactivation of Cys47, a regulatory mechanism that acts as a sensor for oxidative stress. | ||
| + | To visualize the detailed steps of this process, click here for a scene showing the [[_Prx3_Catalytic_Cycle_ | catalytic cycle of a typical 2-Cys peroxiredoxin]]. This scene should illustrate: | ||
== Disease == | == Disease == | ||
Revision as of 01:11, 23 June 2025
Peroxiredoxin 3 (Prx3), Human
Peroxiredoxin 3 (Prx3) is a crucial antioxidant enzyme primarily found in the mitochondria, where it plays a vital role in protecting cells from oxidative stress. It belongs to the 2-Cys peroxiredoxin family, characterized by two key cysteine residues essential for its function. Prx3 reduces harmful hydrogen peroxide (H₂O₂) and organic hydroperoxides to water and alcohol, respectively, thereby maintaining cellular redox balance and influencing processes like apoptosis. Its unique mitochondrial localization makes it a key player in managing reactive oxygen species (ROS) produced during cellular respiration.
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