ENZYME entry: EC 220.127.116.11
View entry in original ENZYME format
View entry in raw text format (no links)
|Mycoredoxin + ROOH <=> mycoredoxin disulfide + H(2)O + ROH|
- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant
- They can be divided into three classes: typical 2-Cys, atypical 2-Cys
and 1-Cys peroxiredoxins.
- The peroxidase reaction comprises two steps centered around a redox-
active cysteine called the peroxidatic cysteine.
- 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).
- The second step of the peroxidase reaction, the regeneration of
cysteine from S-hydroxycysteine, distinguishes the three
- 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 completing the catalytic
- 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.
- The 1-Cys Prxs conserve only the peroxidatic cysteine, so its
regeneration involves direct interaction with a reductant molecule.
- Mycoredoxin-dependent enzymes are found in Mycobacteria.
- Following the reduction of the substrate, the sulfenic acid
derivative of the peroxidatic cysteine forms a protein mixed
disulfide with the N-terminal cysteine of mycoredoxin, which is then
reduced by the C-terminal cysteine of mycoredoxin, restoring the
peroxiredoxin to active state and resulting in an intra-protein
disulfide in mycoredoxin.
- The disulfide is eventually reduced by mycothiol.
- Formerly EC 18.104.22.168.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 1.11.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.11.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-