show all | hide all No of entries

Information on EC 1.11.1.29 - mycoredoxin-dependent peroxiredoxin

for references in articles please use BRENDA:EC1.11.1.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.29 mycoredoxin-dependent peroxiredoxin
IUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred 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) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. 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 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. 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.
Specify your search results
Select one or more organisms in this record: ?
Word Map
The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis
Reaction Schemes
mycoredoxin
+
=
mycoredoxin disulfide
+
+
Synonyms
AhpE, alkyl hydroperoxide reductase E, alkyl hydroxyperoxide reductase E, mycothiol/mycoredoxin-1-dependent peroxidase, peroxiredoxin AhpE, Rv2238c, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
mycoredoxin + ROOH = mycoredoxin disulfide + H2O + ROH
show the reaction diagram
-
-
-
-
Select items on the left to see more content.