http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID239511
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3. |
| title | GRX_GRXh_1_2_like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28785287 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/966851 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30805099 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11896487 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9221819 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21265392 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/870175 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/303426 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26809369 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11109341 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15280699 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 23.