Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid).,
For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle.,
In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond.,
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.,
The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule.,
The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine.,
The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes.,
They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins.,
To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor.
|
| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
AhpC,
Alkyl hydroperoxide reductase C22,
PRDX,
Peroxiredoxin,
Prx,
TXNPx,
Thioredoxin peroxidase,
TrxPx,
Tryparedoxin peroxidase
|
| uniprot:activity |
2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
|