Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Aeropyrum pernix |
Protein Variants | Comment | Organism |
---|---|---|
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 |
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 |
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 |
C50S | no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity | Aeropyrum pernix |
C50S/C207S | no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity | Aeropyrum pernix |
C50S/C213S | mutant enzyme only exists in the monomeric form. No peroxidase activity | Aeropyrum pernix |
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.072 | - |
H2O2 | pH 7.0, 80°C, wild-type enzyme | Aeropyrum pernix | |
0.209 | - |
H2O2 | pH 7.0, 80°C, C207S mutant enzyme | Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9Y9L0 | - |
- |
Aeropyrum pernix DSM 11879 | Q9Y9L0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Aeropyrum pernix |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 thioredoxin + H2O2 | - |
Aeropyrum pernix | thioredoxin disulfide + 2 H2O | - |
? | |
2 thioredoxin + H2O2 | - |
Aeropyrum pernix DSM 11879 | thioredoxin disulfide + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
APE2278 | - |
Aeropyrum pernix |
ApTPx | - |
Aeropyrum pernix |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
assay at | Aeropyrum pernix |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Aeropyrum pernix |
Organism | Comment | Expression |
---|---|---|
Aeropyrum pernix | induced as a cellular adaptation in response to the addition of exogenous H2O2 | up |