| AhpC-TSA | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of AhpC, a bacterial 2-cysteine peroxiredoxin from Salmonella typhimurium. | |||||||||
| Identifiers | |||||||||
| Symbol | AhpC-TSA | ||||||||
| Pfam | PF00578 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR000866 | ||||||||
| SCOP2 | 1prx / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 131 | ||||||||
| OPM protein | 1xvw | ||||||||
| |||||||||
| peroxiredoxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.11.1.15 | ||||||||
| CAS no. | 207137-51-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Peroxiredoxins (Prxs, EC 1.11.1.15; HGNC root symbol PRDX) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels and thereby mediate signal transduction in mammalian cells. The family members in humans are PRDX1, PRDX2, PRDX3, PRDX4, PRDX5, and PRDX6. The physiological importance of peroxiredoxins is indicated by their relative abundance (one of the most abundant proteins in erythrocytes after hemoglobin is peroxiredoxin 2). Their function is the reduction of peroxides, specifically hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite.[1]
- ^ Rhee, Sue Goo; Kil, In Sup (2017). "Multiple Functions and Regulation of Mammalian Peroxiredoxins". Annual Review of Biochemistry. 86: 749–775. doi:10.1146/annurev-biochem-060815-014431. PMID 28226215.