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Results 1 - 9 of 9
EC Number
Natural Substrates
Commentary (Nat. Sub.)
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catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
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peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
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peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
Results 1 - 9 of 9