http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID239311
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs. |
| title | PRX5_like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17291327 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15276456 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21999791 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32765699 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5790483 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19289265 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/33491129 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2978048 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
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