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Field | Value |
---|---|
Namespace | Molecular function |
Short description | Sulfiredoxin activity |
Full defintion | Catalysis of the reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R. |
Subterm of |
The relationship of GO:0032542 with other GO terms.
Relationship type | GO terms |
---|---|
Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0032542, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
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EC | 1.8.98.2 |
PMID | Sulfiredoxin: a potential therapeutic agent? Biomed Pharmacother. 2005 Aug; 59 (7): 374–9.PMID: 16102934 The importance of antioxidants in maintaining homeostasis has long been accepted and includes antioxidant proteins such as, peroxiredoxin (Prx), superoxide dismutase and glutathione S transferases. Sulfiredoxin (Srx) is a recently identified antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. It was first characterized for its regulation of Prx(s) through reduction of the conserved cysteine from sulfinic to sulfenic acid, thereby impacting the role of Prx in regulation of downstream transcription factors and kinase signaling pathways. Furthermore, the reduction of sulfinic to sulfenic acid prevents further oxidation of the conserved cysteine residue to sulfonic acid, the end result of which is degradation. 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. The regulation of glutathionylation/deglutathionylation (or thiol switch) has been likened to phosphorylation/dephosphorylation, another post-translational modification involved in the regulation of signaling pathways. Unlike, the reduction of Prx over-oxidation, Srx-dependent deglutathionylation appears to be non-specific. Deglutathionylation of multiple proteins has been observed both in vitro and in vivo in response to oxidative and/or nitrosative stress. This review discusses Srx as a novel antioxidant, and focuses on its potential role in the regulation of glutathionylation/deglutathionylation pathways, that have been implicated in a growing number of disease states. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | PREDICTED: sulfiredoxin, chloroplastic/mitochondrial-like [Fragaria vesca subsp]. vesca] gi|470115153|ref|XP_004293767.1| | 2 | ||
– | Sulfiredoxin; TAIR: AT1G31170.1 sulfiredoxin; Swiss-Prot: sp|Q8GY89|SRX_ARATH Sulfiredoxin, chloroplastic/mitochondrial; TrEMBL-Plants: tr|I3T533|I3T533_LOTJA Sulfiredoxin; Found in the gene: LotjaGi4g1v0083000 | 2 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Biological process | Oxidation-reduction process | 1 | 50.00 |