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ENZYME entry: EC 1.11.1.28

Accepted Name
Lipoyl-dependent peroxiredoxin.
Reaction catalysed
A [lipoyl-carrier protein]-N(6)-((R)-dihydrolipoyl)-L-lysine + ROOH <=> a [lipoyl-carrier protein]-N(6)-((R)-lipoyl)-L-lysine + 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 (2).
  • 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.
  • Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria.
  • One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis.
  • In that system, AhpC catalyzes reduction of the substrate, resulting in an intramolecular disulfide.
  • AhpD then forms an intermolecular disulfide crosslink with AhpC, reducing it back to active state.
  • AhpD is reduced in turn by lipoylated proteins.
  • The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins.
  • Formerly EC 1.11.1.15.
Cross-references
BRENDA1.11.1.28
EC2PDB1.11.1.28
ExplorEnz1.11.1.28
PRIAM enzyme-specific profiles1.11.1.28
KEGG Ligand Database for Enzyme Nomenclature1.11.1.28
IUBMB Enzyme Nomenclature1.11.1.28
IntEnz1.11.1.28
MEDLINEFind literature relating to 1.11.1.28
MetaCyc1.11.1.28
UniProtKB/Swiss-Prot
A0R1V9, AHPC_MYCS2;  P9WQB6, AHPC_MYCTO;  P9WQB7, AHPC_MYCTU;  
C1F4K1, AHPD_ACIC5;  B8J9Z2, AHPD_ANAD2;  Q2IMQ8, AHPD_ANADE;  
A7HCA3, AHPD_ANADF;  B4UA87, AHPD_ANASK;  A8HQP5, AHPD_AZOC5;  
B2IHZ4, AHPD_BEII9;  Q9ANL0, AHPD_BRADU;  A5ENR3, AHPD_BRASB;  
A4YYT0, AHPD_BRASO;  B2SAW2, AHPD_BRUA1;  Q2YKW2, AHPD_BRUA2;  
Q578J2, AHPD_BRUAB;  A9MBZ4, AHPD_BRUC2;  Q8YCF2, AHPD_BRUME;  
A9WZ04, AHPD_BRUSI;  Q8FVW4, AHPD_BRUSU;  Q9A268, AHPD_CAUVC;  
B8GVX4, AHPD_CAUVN;  C3PGV9, AHPD_CORA7;  Q6NGT4, AHPD_CORDI;  
C4LJ26, AHPD_CORK4;  B6IZ19, AHPD_COXB2;  A9KBI4, AHPD_COXBN;  
A9N917, AHPD_COXBR;  Q83BM5, AHPD_COXBU;  Q0RH96, AHPD_FRAAA;  
A8L1J2, AHPD_FRASN;  A9H8D2, AHPD_GLUDA;  Q0BUC5, AHPD_GRABC;  
Q0BXT2, AHPD_HYPNA;  Q1IJ49, AHPD_KORVE;  Q0AKM4, AHPD_MARMM;  
B0UAJ8, AHPD_METS4;  B8EJZ2, AHPD_METSB;  A0QGI9, AHPD_MYCA1;  
B1MJX0, AHPD_MYCA9;  P0A5N5, AHPD_MYCBO;  A1KLC4, AHPD_MYCBP;  
C1AQZ5, AHPD_MYCBT;  B2HD59, AHPD_MYCMM;  Q73ZL4, AHPD_MYCPA;  
Q50441, AHPD_MYCS2;  A5U5C5, AHPD_MYCTA;  P9WQB4, AHPD_MYCTO;  
P9WQB5, AHPD_MYCTU;  A0PSD4, AHPD_MYCUA;  Q5YT53, AHPD_NOCFA;  
A6X5N3, AHPD_OCHA4;  B6IQZ3, AHPD_RHOCS;  C0ZYQ9, AHPD_RHOE4;  
Q07I00, AHPD_RHOP5;  Q20Y19, AHPD_RHOPB;  Q02BZ5, AHPD_SOLUE;  
A5VCB6, AHPD_SPHWW;  Q82IC5, AHPD_STRAW;  Q7AKI6, AHPD_STRCO;  
B1W2G7, AHPD_STRGG;  Q9X5V1, AHPD_STRVD;  

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