IG. 3. Thioredoxin–peroxiredoxin (TRX-PRDX) system. PRDXs catalyze the reduction of hydrogen peroxide (H 2 O 2 ) to H 2 O. H 2 O 2 oxidizes the peroxidatic cysteine of PRDXs to protein sulfenic acid (PSOH), which can react with the thiol (SH) group of the resolving Cys to yield the formation of an inter-(typical) or intramolecular (atypical) disulfide bond. TRX/ thioredoxin reductase (TRXR) system mediates the reduction of the PRDX disulfide bond. TRX reduced state is maintained by the flavoenzyme TRXR in the presence of NADPH. When H 2 O 2 exceeds the normal levels, PRDXs are overoxidized from PSOH to protein sulfinic acids (PSO 2 H). The latter can be reduced back to the native form of the enzyme by sulfiredoxin (SRX) in the presence of ATP. However, further oxidation of PRDXs to PSO 3 H is irreversible.
måndag 23 oktober 2017
Tioredoxiinin ja peroxiredoxiinin järjestelmä
https://www.researchgate.net/figure/221865379_fig1_FIG-3-Thioredoxin-peroxiredoxin-TRX-PRDX-system-PRDXs-catalyze-the-reduction-of
IG. 3. Thioredoxin–peroxiredoxin (TRX-PRDX) system. PRDXs catalyze the reduction of hydrogen peroxide (H 2 O 2 ) to H 2 O. H 2 O 2 oxidizes the peroxidatic cysteine of PRDXs to protein sulfenic acid (PSOH), which can react with the thiol (SH) group of the resolving Cys to yield the formation of an inter-(typical) or intramolecular (atypical) disulfide bond. TRX/ thioredoxin reductase (TRXR) system mediates the reduction of the PRDX disulfide bond. TRX reduced state is maintained by the flavoenzyme TRXR in the presence of NADPH. When H 2 O 2 exceeds the normal levels, PRDXs are overoxidized from PSOH to protein sulfinic acids (PSO 2 H). The latter can be reduced back to the native form of the enzyme by sulfiredoxin (SRX) in the presence of ATP. However, further oxidation of PRDXs to PSO 3 H is irreversible.
IG. 3. Thioredoxin–peroxiredoxin (TRX-PRDX) system. PRDXs catalyze the reduction of hydrogen peroxide (H 2 O 2 ) to H 2 O. H 2 O 2 oxidizes the peroxidatic cysteine of PRDXs to protein sulfenic acid (PSOH), which can react with the thiol (SH) group of the resolving Cys to yield the formation of an inter-(typical) or intramolecular (atypical) disulfide bond. TRX/ thioredoxin reductase (TRXR) system mediates the reduction of the PRDX disulfide bond. TRX reduced state is maintained by the flavoenzyme TRXR in the presence of NADPH. When H 2 O 2 exceeds the normal levels, PRDXs are overoxidized from PSOH to protein sulfinic acids (PSO 2 H). The latter can be reduced back to the native form of the enzyme by sulfiredoxin (SRX) in the presence of ATP. However, further oxidation of PRDXs to PSO 3 H is irreversible.
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