1.11.1.29: mycoredoxin-dependent peroxiredoxin

This is an abbreviated version!
For detailed information about mycoredoxin-dependent peroxiredoxin, go to the full flat file.

Reaction

Synonyms

AhpE, alkyl hydroperoxide reductase E, alkyl hydroxyperoxide reductase E, EC 1.11.1.15, mycothiol/mycoredoxin-1-dependent peroxidase, peroxiredoxin AhpE, Rv2238c

ECTree

     1 Oxidoreductases

         1.11 Acting on a peroxide as acceptor

             1.11.1 Peroxidases

                1.11.1.29 mycoredoxin-dependent peroxiredoxin

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3	AA Sequence
1	Cloned(Commentary)
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2	General Information
2	Localization
10	Natural Substrates/ Products (Substrates)
16	Organism
12	Protein Variants
1	Purification (Commentary)
1	Reaction
10	Reference
27	Substrates and Products (Substrate)
3	Subunits
23	Synonyms
1	Systematic Name

Systematic Name

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Systematic Name on EC 1.11.1.29 - mycoredoxin-dependent peroxiredoxin

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SYSTEMATIC NAME

IUBMB Comments

mycoredoxin:hydroperoxide oxidoreductase

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 [1]. 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.