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Information on EC 1.8.1.9 - thioredoxin-disulfide reductase

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EC Tree
IUBMB Comments
A flavoprotein (FAD).
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This record set is specific for:
UNIPROT: Q8BTW3
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
thioredoxin reductase, trxr, trxr1, txnrd1, thioredoxin reductase 1, trxr2, txnrd2, thioredoxin reductase-1, thioredoxin reductase 2, nadph-dependent thioredoxin reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thioredoxin reductase
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general stress protein 35
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GSP35
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NADP-thioredoxin reductase
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NADPH-thioredoxin reductase
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-
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NADPH2:oxidized thioredoxin oxidoreductase
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reductase, thioredoxin
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-
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thioredoxin reductase (NADPH)
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9074-14-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
show the reaction diagram
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.47 - 2.72
5,5'-dithiobis(2-nitrobenzoic acid)
0.032 - 0.123
thioredoxin disulfide
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.6 - 20.83
5,5'-dithiobis(2-nitrobenzoic acid)
0.083 - 37
thioredoxin disulfide
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
wild-type enzyme
8
mutant enzyme Sec489C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
pH 6.5: about 40% of maximal activity, pH 9.0: about 50% of maximal activity, wild-type enzyme
6.5 - 9.5
pH 6.5: 45% of maximal activity, pH 9.5: about 50% of maximal activity, mutant enzyme Sec489C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EXOS6_MOUSE
273
0
28370
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sec489C
pH-optimum shifts from pH 7.0 to 8.0
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the full-length Sec489Cys mutant as well as the truncated mTR3 missing the C-terminal CUG tripeptide sequence is expressed as a TR-intein-chitin binding domain fusion protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eckenroth, B.E.; Rould, M.A.; Hondal, R.J.; Everse, S.J.
Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases
Biochemistry
46
4694-4705
2007
Drosophila melanogaster (P91938), Drosophila melanogaster, Mus musculus (Q8BTW3), Mus musculus
Manually annotated by BRENDA team
Eckenroth, B.E.; Lacey, B.M.; Lothrop, A.P.; Harris, K.M.; Hondal, R.J.
Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis
Biochemistry
46
9472-9483
2007
Caenorhabditis elegans, Drosophila melanogaster, Mus musculus (Q8BTW3), Mus musculus
Manually annotated by BRENDA team