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ENZYME entry: EC 1.11.1.26

Accepted Name
NADH-dependent peroxiredoxin.
Alternative Name(s)
Alkyl hydroperoxide reductase.
Reaction catalysed
NADH + ROOH + H(+) <=> NAD(+) + H(2)O + ROH
Comment(s)
  • 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 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 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.
  • Formerly EC 1.11.1.15.
Cross-references
BRENDA1.11.1.26
EC2PDB1.11.1.26
ExplorEnz1.11.1.26
PRIAM enzyme-specific profiles1.11.1.26
KEGG Ligand Database for Enzyme Nomenclature1.11.1.26
IUBMB Enzyme Nomenclature1.11.1.26
IntEnz1.11.1.26
MEDLINEFind literature relating to 1.11.1.26
MetaCyc1.11.1.26
UniProtKB/Swiss-Prot
P82954, AHPC_ACICA;  K0J4Q8, AHPC_AMPXN;  P26830, AHPC_BACAY;  
P80239, AHPC_BACSU;  P57279, AHPC_BUCAI;  Q8K9W0, AHPC_BUCAP;  
Q89AS1, AHPC_BUCBP;  P83117, AHPC_DELAC;  P0AE10, AHPC_ECO57;  
P0AE09, AHPC_ECOL6;  P0AE08, AHPC_ECOLI;  P56876, AHPC_HELPJ;  
P21762, AHPC_HELPY;  Q02UU0, AHPC_PSEAB;  P72314, AHPC_RHORU;  
P0A252, AHPC_SALTI;  P0A251, AHPC_SALTY;  P0AE11, AHPC_SHIFL;  
Q2FJN4, AHPC_STAA3;  P0A0B7, AHPC_STAA8;  Q2YVK2, AHPC_STAAB;  
Q5HIR5, AHPC_STAAC;  P0A0B5, AHPC_STAAM;  P99074, AHPC_STAAN;  
Q6GJR7, AHPC_STAAR;  Q6GC91, AHPC_STAAS;  P0A0B6, AHPC_STAAW;  
Q5HRY1, AHPC_STAEQ;  Q8CMQ2, AHPC_STAES;  Q4L376, AHPC_STAHJ;  
Q49UT8, AHPC_STAS1;  

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