Literature summary for 1.8.1.9 extracted from

Prongay, A.J.; Engelke, D.R.; Williams, C.H.
Characterization of two active site mutations of thioredoxin reductase from Escherichia coli [published erratum appears in J Biol Chem 1989 Jul 15;264(20):12113] (1989), J. Biol. Chem., 264, 2656-2664.

Search for more literature for 1.8.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutant enzymes from plasmids	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C136S	site-directed mutagenesis, reduced activity	Escherichia coli
C139S	site-directed mutagenesis, reduced activity	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00088	-	thioredoxin	mutant C136S	Escherichia coli
0.00125	-	thioredoxin	wild-type	Escherichia coli
0.0017	-	thioredoxin	mutant C139S	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	enzyme with active site mutation	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type from overexpressing cell line, mutants	Escherichia coli

Reaction

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
thioredoxin + NADP+	coupled assay with DTNB	Escherichia coli	thioredoxin disulfide + NADPH	-	r

Synonyms

Synonyms	Comment	Organism
TR	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.38	-	thioredoxin	mutant C136S	Escherichia coli
13.2	-	thioredoxin	mutant C139S	Escherichia coli
22	-	thioredoxin	wild-type	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Escherichia coli
NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)