Thioredoxin
| Human thioredoxin | ||
|---|---|---|
|
||
| Ribbon model (right), surface model (left) of the thioredoxin dimer (reduced form) according to PDB 1AIU . Catalytic amino acids 35–37 shown as domes. | ||
| Properties of human protein | ||
| Mass / length primary structure | 104 amino acids | |
| Secondary to quaternary structure | Homodimer | |
| Identifier | ||
| Gene names | TXN ; TRDX; TRX | |
| External IDs | ||
| Occurrence | ||
| Homology family | Thioredoxin | |
| Parent taxon | Creature | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 7295 | 22166 |
| Ensemble | ENSG00000136810 | ENSMUSG00000028367 |
| UniProt | P10599 | P10639 |
| Refseq (mRNA) | NM_001244938 | NM_011660 |
| Refseq (protein) | NP_001231867 | NP_035790 |
| Gene locus | Chr 9: 110.24 - 110.26 Mb | Chr 4: 57.94 - 57.96 Mb |
| PubMed search | 7295 |
22166
|
Thioredoxins are small proteins with around 100 amino acids and a disulfide bridge as an active center, which are of great importance as electron-transferring cofactors in practically all organisms. In the reduced form, thioredoxins act enzymatically as oxidoreductase . Two thioredoxins are known in humans, depending on their location in the cytoplasm or the mitochondria . From studies in rats there is evidence of a role as an antioxidant and regulator of biomechanical signal transduction . Thioredoxin is not to be confused with the family of proteins that contain a thioredoxin domain . Thioredoxin binds to TXNIP .
In plants, thioredoxins play a key role in the regulation of the primary carbon change: They control the activity of enzymes of the Calvin cycle , the Rubisco activase, and support the assembly of the CF1 subunit of the ATP synthase .
structure
Thioredoxins weigh about 12 kDa . In their active center, which is directed outwards, they carry the sequence cysteine - glycine - proline - cysteine , which is responsible for the electron transfers . The two cysteine groups can assume two different redox states: In oxidized thioredoxin, the cysteine residues are linked to form a disulfide bridge , and there are two reduced SH groups in the enzyme.
Individual evidence
- ↑ Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC0172. Thioredoxin family. Retrieved August 12, 2011 .
- ↑ Thioredoxin. In: Online Mendelian Inheritance in Man . (English)