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

BRENDA support

Literature summary extracted from

  • Wang, P.F.; Marcinkeviciene, J.; Williams, C.H., Jr.; Blanchard, J.S.
    Thioredoxin Reductase-Thioredoxin Fusion Enzyme from Mycobacterium leprae: Comparison with the Separately Expressed Thioredoxin Reductase (1998), Biochemistry, 37, 16378-16389.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.9 expression of wild-type fusion protein and truncated mutant Mycobacterium leprae
1.8.1.9 subunit complex of enzyme via C135 with thioredoxin C32, mutant complex S135-S32, expression from plasmid Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.9 additional information
-
 Escherichia coli
1.8.1.9 additional information thioredoxin is cut off the native fusion protein thioredoxin-thioredoxin reductase resulting in enhanced activity Mycobacterium leprae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.9 iodacetamide
-
 Mycobacterium leprae

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Escherichia coli
-
-
-
1.8.1.9 Mycobacterium leprae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.9 recombinant wild-type fusion protein and truncated mutant Mycobacterium leprae
1.8.1.9 wild-type from plasmid Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.9 thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ oxidation-reduction cycle of thioredoxin Escherichia coli
a
1.8.1.9 thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ oxidation-reduction cycle of thioredoxin Mycobacterium leprae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 1,4-naphthoquinone + NADPH + H+
-
 Mycobacterium leprae ?
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH native thioredoxin-thioredoxin reductase fusion protein Mycobacterium leprae 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Mycobacterium leprae 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Escherichia coli 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Mycobacterium leprae 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 thioredoxin + NADP+ native thioredoxin-thioredoxin reductase fusion protein Mycobacterium leprae thioredoxin disulfide + NADPH
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Escherichia coli thioredoxin disulfide + NADPH
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Mycobacterium leprae thioredoxin disulfide + NADPH
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.9 7
-
-
 Escherichia coli
1.8.1.9 7
-
 wild-type fusion protein Mycobacterium leprae
1.8.1.9 9
-
 around, mutant enzyme, broad optimum Mycobacterium leprae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.8.1.9 5.5 9 wild-type fusion protein Mycobacterium leprae
1.8.1.9 6.5 10 mutant enzyme, 50% activity at pH 6.5 Mycobacterium leprae

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD
-
 Escherichia coli
1.8.1.9 FAD
-
 Mycobacterium leprae
1.8.1.9 NADPH
-
 Escherichia coli
1.8.1.9 NADPH
-
 Mycobacterium leprae