1.11.1.25: glutaredoxin-dependent peroxiredoxin

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

Reaction

Synonyms

EC 1.11.1.15, glutaredoxin-dependent peroxidase, Grx3/GSH-dependent peroxidase, peroxiredoxin-glutaredoxin, Prx1, Prx3, Prx5-Grx, PRXIIB, TM0780, TmPrxBCP, TmPrxNtr, TM_0386, type II peroxiredoxin

ECTree

     1 Oxidoreductases

         1.11 Acting on a peroxide as acceptor

             1.11.1 Peroxidases

                1.11.1.25 glutaredoxin-dependent peroxiredoxin

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Results	in table
1555	AA Sequence
7	Cloned(Commentary)
2	Expression
12	General Information
1	Inhibitors
2	kcat/KM [mM/s]
8	KM Value [mM]
5	Localization
4	Molecular Weight [Da]
13	Organism
2	pH Optimum
1	pH Range
17	Protein Variants
4	Purification (Commentary)
1	Reaction
11	Reference
2	Source Tissue
20	Substrates and Products (Substrate)
6	Subunits
24	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
7	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.11.1.25 - glutaredoxin-dependent peroxiredoxin

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SYSTEMATIC NAME

IUBMB Comments

glutaredoxin: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 [2]. 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. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals. These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.