Glutathione peroxidase
Glutathione peroxidase 1 | ||
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Belt and surface model according to PDB 2F8A | ||
Properties of human protein | ||
Mass / length primary structure | 201 AS ; 21.9 kDa | |
Secondary to quaternary structure | Homotetramer | |
Identifier | ||
Gene names | GPX1 ; GSHPX-1 | |
External IDs |
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Enzyme classification | ||
EC, category | 1.11.1.9 , oxidoreductase | |
Response type | Redox reaction | |
Substrate | 2 glutathione + H 2 O 2 | |
Products | Glutathione disulfide + 2 H 2 O | |
Occurrence | ||
Homology family | Thioredoxin | |
Parent taxon | Creature |
The glutathione peroxidases catalyze the glutathione- dependent reduction of organic peroxides and hydrogen peroxide . In the catalytic center they carry L - selenocysteine , a derivative of L - serine or L - cysteine . The phospholipid hydroperoxide glutathione peroxidase belongs to the family of glutathione peroxidases.
Glutathione peroxidases are particularly important as a component of the cellular defense against the consequences of oxidative stress . Disturbances in the function of such selenoproteins go hand in hand with deficiency syndromes such as Keshan and Kashin-Beck disease and may play a role in tumor development, in atherosclerosis and - in conjugation with 4-hydroxynonenals - in neurodegenerative diseases .
Catalyzed reaction
The reaction can be roughly divided into the following individual steps:
Enzyme-Selenocysteine-SeH + H 2 O 2 Enzyme-Selenocysteine-SeOH + H 2 O
Enzyme-Selenocysteine-SeOH + GSH GS-Se-Selenocysteine-Enzyme + H 2 O
GS-Se-Selenocysteine-Enzyme + GSH Enzyme-Selenocysteine-SeH + GSSG
The overall reaction is:
2 GSH + H 2 O 2 2 H 2 O + GSSG
The glutathione disulfide (GSSG) produced during the reaction is regenerated into two molecules of glutathione by the enzyme glutathione disulfide reductase using NADPH / H + as a reducing agent.
Web links
Individual evidence
- ↑ K. Aoyama, K. Matsubara, S. Kobayashi: Aging and oxidative stress in progressive supranuclear palsy . In: Eur J Neurol. 13 (1), Jan 2006, pp. 89-92. (engl.)