Peroxiredoxin: Difference between revisions
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{{STRUCTURE_1qq2| PDB=1qq2 | SIZE=400| SCENE= |right|CAPTION= | {{STRUCTURE_1qq2| PDB=1qq2 | SIZE=400| SCENE= |right|CAPTION=Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]}} | ||
== Function == | == Function == | ||
[[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. | [[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. | ||
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== Relevance == | == Relevance == | ||
Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | ||
== Structural highlights == | |||
In the typical 2-cysteine Prx the Cys-Cys bond is formed between two subunits<ref>PMID:10535922</ref>. | |||
== 3D Structures of Peroxiredoxin == | == 3D Structures of Peroxiredoxin == | ||
