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

BRENDA support

Literature summary for 1.8.1.9 extracted from

  • Williams, C.H.
    Flavin-containing dehydrogenases (1976), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 13, 89-173.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
phosphate 2fold activation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADP+ product inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0008
-
NADPH at 4°C Escherichia coli
0.0012
-
NADPH at 25°C Escherichia coli
0.0017
-
thioredoxin at 4°C Escherichia coli
0.0028
-
thioredoxin at 25°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
sedimentation equilibrium analysis Escherichia coli
73000 75000 amino acid analysis based on 2 mol FAD per molecule of enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thioredoxin + NADP+ Escherichia coli metabolic function of thioredoxin reductase-thioredoxin system: supplies reducing equivalents for a wide variety of acceptors, e.g. : ribonucleotide reductase, nonspecific protein disulfide reductase, methionine sulfoxide reductase, D-proline reductase thioredoxin disulfide + NADPH
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7 Escherichia coli ?
-
?
additional information reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7 Escherichia coli B / ATCC 11303 ?
-
?
additional information reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7 Escherichia coli Crookes ?
-
?
additional information reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7 Escherichia coli M191-6 ?
-
?
thioredoxin + NADP+ wide variety of electron acceptors Escherichia coli thioredoxin disulfide + NADPH
-
?
thioredoxin + NADP+ metabolic function of thioredoxin reductase-thioredoxin system: supplies reducing equivalents for a wide variety of acceptors, e.g. : ribonucleotide reductase, nonspecific protein disulfide reductase, methionine sulfoxide reductase, D-proline reductase Escherichia coli thioredoxin disulfide + NADPH
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
about Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD 2 FAD per dimer Escherichia coli
NADPH specific for Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.015
-
NADP+ at 25°C Escherichia coli