Peroxiredoxin 5: Structure, Mechanism, and Function of the Mammalian Atypical 2-Cys Peroxiredoxin
| Autor: | Jean-Paul Declercq, Valérie Van der Eecken, Bernard Knoops, Julie Goemaere |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Protein Conformation
Physiology Molecular Sequence Data Clinical Biochemistry Mitochondrion Biology Crystallography X-Ray Biochemistry Structure-Activity Relationship chemistry.chemical_compound Protein structure Catalytic Domain Animals Humans Amino Acid Sequence Cysteine Molecular Biology General Environmental Science PRDX5 Hydrogen Peroxide Peroxiredoxins Cell Biology Peroxisome Cell biology Kinetics Cytosol chemistry biology.protein General Earth and Planetary Sciences Peroxiredoxin Peroxynitrite Peroxidase |
| Zdroj: | Antioxidants & Redox Signaling. 15:817-829 |
| ISSN: | 1557-7716 1523-0864 |
| DOI: | 10.1089/ars.2010.3584 |
| Popis: | Peroxiredoxin 5 (PRDX5) was the last member to be identified among the six mammalian peroxiredoxins. It is also the unique atypical 2-Cys peroxiredoxin in mammals. Like the other five members, PRDX5 is widely expressed in tissues but differs by its surprisingly large subcellular distribution. In human cells, it has been shown that PRDX5 can be addressed to mitochondria, peroxisomes, the cytosol, and the nucleus. PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce alkyl hydroperoxides or peroxynitrite with high rate constants in the 10(6) to 10(7) M(-1)s(-1) range, whereas its reaction with hydrogen peroxide is more modest, in the 10(5) M(-1)s(-1) range. PRDX5 crystal structures confirmed the proposed enzymatic mechanisms based on biochemical data but revealed also some specific unexpected structural features. So far, PRDX5 has been viewed mainly as a cytoprotective antioxidant enzyme acting against endogenous or exogenous peroxide attacks rather than as a redox sensor. Accordingly, overexpression of the enzyme in different subcellular compartments protects cells against death caused by nitro-oxidative stresses, whereas gene silencing makes them more vulnerable. Thus, more than 10 years after its molecular cloning, mammalian PRDX5 appears to be a unique peroxiredoxin exhibiting specific functional and structural features. |
| Databáze: | OpenAIRE |
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