Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.24 extracted from

  • Suttiprapa, S.; Loukas, A.; Laha, T.; Wongkham, S.; Kaewkes, S.; Gaze, S.; Brindley, P.J.; Sripa, B.
    Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini (2008), Mol. Biochem. Parasitol., 160, 116-122.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed as soluble protein in Escherichia coli Opisthorchis viverrini

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23570
-
monomer, calculated from amino acid sequence Opisthorchis viverrini
25000
-
2 * 25000, SDS-PAGE Opisthorchis viverrini
50000
-
non-reducing and non-denaturing SDS-PAGE Opisthorchis viverrini

Organism

Organism UniProt Comment Textmining
Opisthorchis viverrini B4Y9T5
-
-

Purification (Commentary)

Purification (Comment) Organism
TALON metal affinity resin column chromatography Opisthorchis viverrini

Source Tissue

Source Tissue Comment Organism Textmining
adult
-
Opisthorchis viverrini
-
egg
-
Opisthorchis viverrini
-
metacercaria
-
Opisthorchis viverrini
-
additional information TPx is also detected in bile fluid and bile duct epithelial cells surrounding the flukes 2 weeks after infection of hamsters with Opisthorchis viverrini Opisthorchis viverrini
-

Subunits

Subunits Comment Organism
homodimer 2 * 25000, SDS-PAGE Opisthorchis viverrini

Synonyms

Synonyms Comment Organism
thioredoxin peroxidase
-
Opisthorchis viverrini
Tpx
-
Opisthorchis viverrini