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Information on EC 1.8.1.9 - thioredoxin-disulfide reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P29509
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1.8.1.9 thioredoxin-disulfide reductaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.8.1.9
- selenium
-
selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
-
selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
-
redox-active
- cisplatin
- dithiols
-
goldi
-
se-deficient
- dtnb
-
iodothyronine
-
flavoenzyme
- ebselen
-
redox-sensitive
-
selenium-containing
-
selenols
-
deiodinases
-
thiol-dependent
-
organoselenium
-
thioredoxin-like
-
selenium-deficient
-
se-dependent
-
n-heterocyclic
-
thioredoxin-dependent
- diselenide
-
redox-regulated
-
selenium-dependent
-
thiol-disulfide
-
thiol-based
- thioredoxin-1
- ask1
-
carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
-
secis
-
txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
-
thioredoxin-interacting
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Trr1
general stress protein 35
-
-
-
-
GSP35
-
-
-
-
NADP-thioredoxin reductase
-
-
-
-
NADPH-thioredoxin reductase
-
-
-
-
NADPH2:oxidized thioredoxin oxidoreductase
-
-
-
-
reductase, thioredoxin
-
-
-
-
thioredoxin reductase (NADPH)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9074-14-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin 1 + NADP+ +
thioredoxin 1 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 2 + NADP+
thioredoxin 2 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 3 + NADP+
thioredoxin 3 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin-II + NADP+
thioredoxin-II disulfide + NADPH + H+
-
-
-
-
r
additional information
?
-
-
the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin 1 + NADP+ +
thioredoxin 1 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 2 + NADP+
thioredoxin 2 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 3 + NADP+
thioredoxin 3 disulfide + NADPH + H+
-
-
-
-
?
additional information
?
-
-
the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
0.0011
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
0.0006
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
0.0009
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
43.7
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
34
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
42.9
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
47.1
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34000
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
31000
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
52000
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
73000
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
reporter gene transactivation by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. Decreased reporter gene activity in thioredoxin reductase null cells is due to reduced p53 specific activity rather than reduced p53 protein levels
malfunction
-
TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. The autophagy caused by nitrogen starvation is reduced in the trr1DELTA mutant
physiological function
-
Trr2/Trx3 and Trr2/GSH systems exhibit similar capacities for supporting peroxidredoxin 1 catalysis. TRR2 is required for cadmium and hydrogen peroxide resistance promoted by overexpression of peroxiredoxin 1
physiological function
-
thioredoxin reductase Trr1p controls TORC1-regulated processes. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M MES buffer, pH 6.5, 10% (w/v) PEG 20000, at 18°C
hanging drop vapor diffusion method, using 0.1 M MES buffer, pH 6.5, 10% PEG 20000, at 18°C
hanging-drop vapour diffusion in the presence of PEG 3000 as precipitant after treatment with hydrogen peroxide
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gibson, R.M.; Large, P.J.
The involvement of thioredoxin and thioredoxin reductase in the dimethyl sulphoxide reductase system of Saccharomyces cerevisiae
FEMS Microbiol. Lett.
26
89-94
1985
Saccharomyces cerevisiae
-
Speranza, M.L.; Ronchi, S.; Minchiotti, L.
Purification and characterization of yeast thioredoxin reductase
Biochim. Biophys. Acta
327
274-281
1973
Saccharomyces cerevisiae
Oliveira, M.A.; Discola, K.F.; Alves, S.V.; Barbosa, J.A.; Medrano, F.J.; Netto, L.E.; Guimaraes, B.G.
Crystallization and preliminary X-ray diffraction analysis of NADPH-dependent thioredoxin reductase I from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
61
387-390
2005
Saccharomyces cerevisiae
Zhang, Z.; Bao, R.; Zhang, Y.; Yu, J.; Zhou, C.Z.; Chen, Y.
Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin
Biochim. Biophys. Acta
1794
124-128
2009
Saccharomyces cerevisiae (P29509), Saccharomyces cerevisiae
Greetham, D.; Grant, C.M.
Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
Mol. Cell. Biol.
29
3229-3240
2009
Saccharomyces cerevisiae
Stoner, C.S.; Pearson, G.D.; Koc, A.; Merwin, J.R.; Lopez, N.I.; Merrill, G.F.
Effect of thioredoxin deletion and p53 cysteine replacement on human p53 activity in wild-type and thioredoxin reductase null yeast
Biochemistry
48
9156-9169
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Oliveira, M.A.; Discola, K.F.; Alves, S.V.; Medrano, F.J.; Guimaraes, B.G.; Netto, L.E.
Insights into the specificity of thioredoxin reductase-thioredoxin interactions. A structural and functional investigation of the yeast thioredoxin system
Biochemistry
49
3317-3326
2010
Saccharomyces cerevisiae
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