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Information on EC 1.8.1.9 - thioredoxin-disulfide reductase and Organism(s) Drosophila melanogaster and UniProt Accession P91938

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EC Tree
IUBMB Comments
A flavoprotein (FAD).
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This record set is specific for:
Drosophila melanogaster
UNIPROT: P91938
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thioredoxin reductase
-
EC 1.6.4.5
-
formerly
general stress protein 35
-
-
-
-
GSP35
-
-
-
-
NADP-thioredoxin reductase
-
-
-
-
NADPH-thioredoxin reductase
-
-
-
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NADPH2:oxidized thioredoxin oxidoreductase
-
-
-
-
reductase, thioredoxin
-
-
-
-
thioredoxin reductase
-
-
thioredoxin reductase (NADPH)
-
-
-
-
thioredoxin reductase-1
-
-
TrxR-1(cyto)
-
-
TrxR-1(mito)
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9074-14-0
-
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
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
show the reaction diagram
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
show the reaction diagram
-
-
-
-
?
methylseleninate + H2O2
?
show the reaction diagram
-
-
-
-
?
NADPH + thioredoxin disulfide
NADP+ + thioredoxin
show the reaction diagram
-
mechanism, Cys57 attacks Cys490 in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
show the reaction diagram
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
show the reaction diagram
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
thioredoxin-1 disulfide + NADPH
NADP+ + thioredoxin-1
show the reaction diagram
-
-
-
-
?
thioredoxin-1 disulfide + NADPH + H+
thioredoxin-1 + NADP+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
thioredoxin + NADP+
thioredoxin disulfide + NADPH
show the reaction diagram
-
defense against oxidative stress
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
show the reaction diagram
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
-
DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2. This process is consistent with the corresponding redox potentials and is essential for GSSG/GSH cycling in Drosophila melanogaster, which is deficient in glutathione reductase
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
selenocysteine-containing enzyme
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 0.92
5,5'-dithiobis(2-nitrobenzoic acid)
0.141
thioredoxin disulfide
full-length Drosophila enzyme with C-terminal sequence SCCS
0.22 - 4.1
5,5'-dithiobis(2-nitrobenzoic acid)
0.38 - 0.41
DTNB
0.001 - 1
NADPH
0.007 - 0.019
thioredoxin
0.173
thioredoxin disulfide
-
pH 7, 25°C
0.007 - 0.019
thioredoxin-1 disulfide
-
additional information
additional information
-
KM-values of truncated enzymes forms
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 2.4
5,5'-dithiobis(2-nitrobenzoic acid)
5.8
thioredoxin disulfide
full-length Drosophila enzyme with C-terminal sequence SCCS
2.62 - 21.6
5,5'-dithiobis(2-nitrobenzoic acid)
12
methylseleninate
-
recombinant protein
4.99
thioredoxin disulfide
-
pH 7, 25°C
additional information
additional information
-
turnover number of truncated enzyme forms
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 5.27
5,5'-dithiobis(2-nitrobenzoic acid)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.93
-
TrxR-1(cyto)
8.15
-
TrxR-1(mito)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRXR1_DROME
596
0
64322
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53200
-
cytosolic TrxR1 isoform, deduced from amino acid sequence
55000
-
12% reducing SDS-PAGE
63700
-
mitochondrial TrxR1 isoform, deduced from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop diffusion method at 20°C, X-ray crystal structure of DmTR at 2.4 A resolution in which the enzyme was truncated to remove the C-terminal tripeptide sequence Cys-Cys-Ser
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H106F
catalytic activity drops considerably yet pH-profile does not reveal differences
H106N
catalytic activity drops considerably yet pH-profile does not reveal differences
H106Q
catalytic activity drops considerably yet pH-profile does not reveal differences
C489S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C489S/C490S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C490S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
E469A
-
the mutant retains 28% of the wild type activity
E469Q
-
the mutant retains 35% of the wild type activity
E470A
-
the mutant retains 70% of the wild type activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
-
recombinant wild-type cytosolic and mitochondrial isoforms and mutants from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli ER2566 cells
-
expression of cytosolic and mitochondrial isoform as His-tagged enzymes in Escherichia coli
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wild-type and C-terminal variants
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, Q.A.; Zappacosta, F.; Factor, V.M.; Wirth, P.J.; Hatfield, D.L.; Gladyshev, V.N.
Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing
J. Biol. Chem.
276
3106-3114
2001
Drosophila melanogaster, Drosophila melanogaster (P91938), Homo sapiens, Homo sapiens (Q9NNW7), Mus musculus, Mus musculus (Q9JMH6), Rattus norvegicus
Manually annotated by BRENDA team
Gromer, S.; Gross, J.H.
Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase: implications for the antitumor effects of selenium
J. Biol. Chem.
277
9701-9706
2002
Drosophila melanogaster, Homo sapiens, Mus musculus, Plasmodium falciparum
Manually annotated by BRENDA team
Missirlis, F.; Ulschmid, J.K.; Hirosawa-Takamori, M.; Gronke, S.; Schafer, U.; Becker, K.; Phillips, J.P.; Jackle, H.
Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability
J. Biol. Chem.
277
11521-11526
2002
Drosophila melanogaster
Manually annotated by BRENDA team
Jacob, J.; Schirmer, R.H.; Gromer, S.
The conserved histidine 106 of large thioredoxin reductases is likely to have a structural role but not a base catalyst function
FEBS Lett.
579
745-748
2005
Drosophila melanogaster (P91938), Drosophila melanogaster
Manually annotated by BRENDA team
Bauer, H.; Massey, V.; Arscott, L.D.; Schirmer, R.H.; Ballou, D.P.; Williams, C.H., Jr.
The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster
J. Biol. Chem.
278
33020-33028
2003
Drosophila melanogaster
Manually annotated by BRENDA team
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
Cheng, Z.; Arscott, L.D.; Ballou, D.P.; Williams, C.H.
The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila
Biochemistry
46
7875-7885
2007
Drosophila melanogaster
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
Huang, H.H.; Arscott, L.D.; Ballou, D.P.; Williams, C.H.
Function of Glu-469 in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster
Biochemistry
47
12769-12776
2008
Drosophila melanogaster
Manually annotated by BRENDA team
Lacey, B.M.; Eckenroth, B.E.; Flemer, S.; Hondal, R.J.
Selenium in thioredoxin reductase: a mechanistic perspective
Biochemistry
47
12810-12821
2008
Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team