User:Eduarda Franco Marcolino/Sandbox 2
From Proteopedia
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==Peroxiredoxin 3 (Prx3), Human== | ==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. | 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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== 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. | 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. | ||
Revision as of 01:27, 23 June 2025
Contents |
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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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 catalytic cycle of a typical 2-Cys peroxiredoxin. This scene should illustrate:
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