1.11.1.26: NADH-dependent peroxiredoxin

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

Reaction

Synonyms

AhpC, AhpC1, AhpCF, AhpF, AhpR, alkyl hydroperoxidase, alkyl hydroperoxide reductase, alkyl hydroperoxide reductase subunit C, alkyl hydroperoxide reductase subunit F, alkyl-hydroperoxide reductase C1, alkylhydroperoxide reductase, alkylhydroperoxide reductase subunit C, EC 1.11.1.15, FTL_1015, FTT_0557, NADH peroxidase, NADH peroxidase alkyl hydroperoxide reductase, peroxiredoxin C, Prx

ECTree

     1 Oxidoreductases

         1.11 Acting on a peroxide as acceptor

             1.11.1 Peroxidases

                1.11.1.26 NADH-dependent peroxiredoxin

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Results	in table
11498	AA Sequence
4	Application
10	Cloned(Commentary)
2	Crystallization (Commentary)
29	General Information
28	kcat/KM [mM/s]
28	KM Value [mM]
8	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
89	Organism
2	PDB ID
2	pH Optimum
33	Protein Variants
11	Purification (Commentary)
3	Reaction
33	Reference
30	Substrates and Products (Substrate)
8	Subunits
72	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
28	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.11.1.26 - NADH-dependent peroxiredoxin

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SYSTEMATIC NAME

IUBMB Comments

NADH: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. This bacterial peroxiredoxin differs from most other forms by comprising two types of subunits. One subunit (AhpC) is a typical 2-Cys peroxiredoxin. Following the reduction of the substrate, one AhpC subunit forms a disulfide bond with an identical unit. The disulfide bond is reduced by the second type of subunit (AhpF). This second subunit is a flavin-containing protein that uses electrons from NADH to reduce the cysteine residues on the AhpC subunits back to their active state.