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Literature summary extracted from

  • Jeon S.J.; Ishikawa, K.
    Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003), J. Biol. Chem., 278, 24174-24180.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 expression in Escherichia coli Aeropyrum pernix

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.24 C207S like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. Peroxidase activity is less effective than the wild type activity Aeropyrum pernix
1.11.1.24 C207S/C213S forms a toroid-shaped structure. The size and shapes of the top view are similar to those of the wild type. The octameric form of C207S/C213S mutant dissociates into monomer in the presence of 10 mM DTT. Peroxidase activity is similar to wilde type activity Aeropyrum pernix
1.11.1.24 C213S like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. No peroxidase activity Aeropyrum pernix
1.11.1.24 C50S no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity Aeropyrum pernix
1.11.1.24 C50S/C207S no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity Aeropyrum pernix
1.11.1.24 C50S/C213S mutant enzyme only exists in the monomeric form. No peroxidase activity Aeropyrum pernix
1.11.1.24 additional information mutagenesis studies suggest that the sulfhydryl group of Cys50 is the site of oxidation by peroxide and that oxidized Cys50 reacts with the sulfhydryl group of Cys213 of another subunit to form an intermolecular disulfide bond. Mutants lacking either Cys50 or Cys213 show no thioredoxin peroxidase activity, whereas the mutant lacking Cys207 has a thioredoxin peroxidase activity Aeropyrum pernix

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.24 0.072
-
 H2O2 pH 7.0, 80°C, wild-type enzyme Aeropyrum pernix
1.11.1.24 0.209
-
 H2O2 pH 7.0, 80°C, C207S mutant enzyme Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Aeropyrum pernix Q9Y9L0
-
-
1.11.1.24 Aeropyrum pernix DSM 11879 Q9Y9L0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24
-
 Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 2 thioredoxin + H2O2
-
 Aeropyrum pernix thioredoxin disulfide + 2 H2O
-
 ?
1.11.1.24 2 thioredoxin + H2O2
-
 Aeropyrum pernix DSM 11879 thioredoxin disulfide + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.24 hexadecamer composed of two identical octamers, 2-fold toroid-shaped structure with outer and inner diameters of 14 and 6 nm, respectively. Although oligomerization of individual subunits does not take place through an intersubunit-disulfide linkage involving Cys50 and Cys213, Cys50 is essential for the formation of the hexadecamer Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 APE2278
-
 Aeropyrum pernix
1.11.1.24 ApTPx
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.24 80
-
 assay at Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.24 7
-
 assay at Aeropyrum pernix

Expression

EC Number Organism Comment Expression
1.11.1.24 Aeropyrum pernix induced as a cellular adaptation in response to the addition of exogenous H2O2 up