Peroxiredoxin: Difference between revisions
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<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'> | <StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' 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. '''Prx Q''' is the plant homolog of [[Bacterioferritin comigratory protein]]. | ||
'''Typical 2-Cys Prx'''<br /> | '''Typical 2-Cys Prx'''<br /> | ||