EC Number   |
General Information |
Reference  |
|---|
   1.8.98.2 | physiological function |
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfinic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx and the conserved Srx is capable of regenerating the functionality of both pea and Arabidopsis Prx-SO2H |
-, 712607 |
| 1.8.98.2 | physiological function |
sulfiredoxin Srx1 reactivates the yeast peroxiredoxin Prx1 peroxidase activity that is inactivated by H2O2, whereas it decreases the chaperone activity enhanced by H2O2. Srx1 dissociates the H2O2-induced high molecular weight Prx1 complex, and the Srx1 Cys84 residue is critical for its dissociation |
724192 |
| 1.8.98.2 | physiological function |
exposure of low steady-state levels ofH2O2 to A-549 or wild-type mouse embryonic fibroblast cells does not lead to any significant change in oxidative injury. Loss-of-function studies using sulfiredoxin-depleted A549 and sulfiredoxin -/- cells demonstrate a dramatic increase in extra- and intracellular H2O2, sulfinic 2-Cys peroxiredoxins, and apoptosis. Concomitant with hyperoxidation of mitochondrial peroxiredoxin Prx III, sulfiredoxin-depleted cells show an activation of mitochondria-mediated apoptotic pathways including mitochondria membrane potential collapse, cytochrome c release, and caspase activation |
725510 |
| 1.8.98.2 | physiological function |
enzyme induction is the pivotal compensatory protection mechanism against oxidative stress in diabetes or hyperglycaemia |
742457 |
| 1.8.98.2 | physiological function |
mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin |
742566 |
| 1.8.98.2 | physiological function |
sulfiredoxin-1 protects PC-12 cells against oxidative stress induced by hydrogen peroxide |
743135 |
| 1.8.98.2 | malfunction |
loss of the extended active site interface within engineered peroxiredoxin isozymes, Prx2 and Prx3, dimers yields variants more resistant to hyperoxidation and repair by enzyme Srx |
763914 |
| 1.8.98.2 | more |
the decameric Srx-Prx1 complex reveals extended binding interface, human Prx1 and Prx2 form a decameric toroid. The crystal structure of the toroidal Prx1-Srx complex shows an extended active site interface. Structural basis for the ability of Srx to reduce the hyperoxidized form of human Prxs, juxtaposition of the two active-site interfaces of the two proteins and wrapping of the Prx C-terminus around Srx in an essential interaction, overview |
763914 |
| 1.8.98.2 | physiological function |
the repair and reactivation of the hyperoxidized Prxs by Srx is an important cellular process, hydrogen sulfide repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx), structural requirements, peroxiredoxin catalytic and sulfiredoxin repair cycles, detailed overview. The physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) show relative efficacy in this reaction. Prx isoform-dependent use of and potential cooperation between GSH and H2S in supporting Srx activity |
763914 |
| 1.8.98.2 | evolution |
AtSrx has more positive charges than human enzyme HsSrx. The theoretical pI of AtSrx is 9.86, much higher than 5.47 of HsSrx. There are 10 arginine residues and 7 lysine residues in AtSrx but only 5 arginine residues and 3 lysine residues in HsSrx. For negatively charged amino acids residues, there are 6 glutamic acid residues and 4 aspartic acid residues in AtSrx, while there are 2 glutamic acid residues and 8 aspartic acid residues in HsSrx. Abundant charged amino acids of AtSrx provide more positive charge at ADP binding pocket and more interaction with active |
764076 |
