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

BRENDA support

Literature summary extracted from

  • Gilberger, T.W.; Walter, R.D.; Muller, S.
    Identification and characterization of the functional amino acids at the active site of the large thioredoxin reductase from Plasmodium falciparum (1997), J. Biol. Chem., 272, 29584-29589.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.9 cysteine at the active center, C88 and C93 Plasmodium falciparum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.9 expression of wild-type and mutants in Escherichia coli Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.9 C88A site-directed mutagenesis, no activity Plasmodium falciparum
1.8.1.9 C88S site-directed mutagenesis, no activity Plasmodium falciparum
1.8.1.9 C93A site-directed mutagenesis, no activity Plasmodium falciparum
1.8.1.9 H509A site-directed mutagenesis, reduced activity Plasmodium falciparum
1.8.1.9 H509Q site-directed mutagenesis, reduced activity Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.9 0.05
-
 DTNB mutant enzyme H509Q Plasmodium falciparum
1.8.1.9 0.147
-
 DTNB mutant enzyme H509A Plasmodium falciparum
1.8.1.9 0.212
-
 DTNB wild-type enzyme Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Plasmodium falciparum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.9 recombinant wild-type and mutants from Escherichia coli Plasmodium falciparum

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.9 thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH Plasmodium falciparum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.9 0.22
-
 mutant H509Q, coupled assay with DTNB Plasmodium falciparum
1.8.1.9 4.3
-
 mutant H509A, coupled assay with DTNB Plasmodium falciparum
1.8.1.9 4.3
-
 wild-type enzyme, coupled assay with DTNB Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Plasmodium falciparum 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Plasmodium falciparum 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Plasmodium falciparum thioredoxin disulfide + NADPH
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin Plasmodium falciparum thioredoxin disulfide + NADPH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 More 2 classes of thioredoxin reductases: high molecular weight or large proteins e.g. in mammalia, Plasmodium falsiparum and Caenorhabditis elegans, and low molecular weight proteins e.g. in bacteria Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.9 20
-
 assay at Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.9 0.16
-
 DTNB mutant enzyme H509A Plasmodium falciparum
1.8.1.9 0.233
-
 DTNB mutant enzyme H509Q Plasmodium falciparum
1.8.1.9 4.58
-
 DTNB wild-type enzyme Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.9 7.4
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD
-
 Plasmodium falciparum
1.8.1.9 NADPH
-
 Plasmodium falciparum