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EC Tree
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
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general stress protein 35
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NADP-thioredoxin reductase
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NADPH-thioredoxin reductase
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NADPH2:oxidized thioredoxin oxidoreductase
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reductase, thioredoxin
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thioredoxin reductase
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thioredoxin reductase (NADPH)
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thioredoxin reductase-1
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thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
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5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
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?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
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?
methylseleninate + H2O2
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?
NADPH + thioredoxin disulfide
NADP+ + thioredoxin
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mechanism, Cys57 attacks Cys490 in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide
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?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
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?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
thioredoxin-1 disulfide + NADPH
NADP+ + thioredoxin-1
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?
thioredoxin-1 disulfide + NADPH + H+
thioredoxin-1 + NADP+
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r
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
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i.e. DTNB
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
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i.e. DTNB
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
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coupled assay
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?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
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coupled assay
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?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
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coupled assay with DTNB
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?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
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coupled assay with DTNB
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r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
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defense against oxidative stress
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?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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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
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r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2
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r
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thioredoxin + NADP+
thioredoxin disulfide + NADPH
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defense against oxidative stress
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?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
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thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
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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
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r
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FAD
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NADPH
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selenium
selenocysteine-containing enzyme
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
additional information
DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
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DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
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TrxR-1(cyto) is not a selenoprotein
additional information
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TrxR-1(mito) is not a selenoprotein
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cysteine
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C-terminal redox active disulfide
cysteine
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part of the active site
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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)
0.007 - 0.019
thioredoxin
0.173
thioredoxin disulfide
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pH 7, 25°C
0.007 - 0.019
thioredoxin-1 disulfide
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additional information
additional information
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KM-values of truncated enzymes forms
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0.17
5,5'-dithiobis(2-nitrobenzoic acid)
full-length Drosophila enzyme with C-terminal sequence SCCS
0.92
5,5'-dithiobis(2-nitrobenzoic acid)
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
0.22
5,5'-dithiobis(2-nitrobenzoic acid)
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wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.75
5,5'-dithiobis(2-nitrobenzoic acid)
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pH 7, 25°C
4.1
5,5'-dithiobis(2-nitrobenzoic acid)
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truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
0.38
DTNB
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cytosolic TrxR1 isoform
0.41
DTNB
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mitochondrial TrxR1 isoform
0.001
NADPH
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cytosolic and mitochondrial TrxR1 isoform
0.007
thioredoxin
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cytosolic TrxR1 isoform
0.019
thioredoxin
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mitochondrial TrxR1 isoform
0.007
thioredoxin-1 disulfide
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TrxR(cyto)
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0.019
thioredoxin-1 disulfide
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TRxR(mito)
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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
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recombinant protein
4.99
thioredoxin disulfide
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pH 7, 25°C
additional information
additional information
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turnover number of truncated enzyme forms
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1.6
5,5'-dithiobis(2-nitrobenzoic acid)
full-length Drosophila enzyme with C-terminal sequence SCCS
2.4
5,5'-dithiobis(2-nitrobenzoic acid)
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
2.62
5,5'-dithiobis(2-nitrobenzoic acid)
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pH 7, 25°C
2.62
5,5'-dithiobis(2-nitrobenzoic acid)
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wild type enzyme, in 50 mM potassium phosphate at pH 7.0
21.6
5,5'-dithiobis(2-nitrobenzoic acid)
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truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
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0.22 - 5.27
5,5'-dithiobis(2-nitrobenzoic acid)
0.22
5,5'-dithiobis(2-nitrobenzoic acid)
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wild type enzyme, in 50 mM potassium phosphate at pH 7.0
5.27
5,5'-dithiobis(2-nitrobenzoic acid)
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truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
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7.1
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cytosolic and mitochondrial TrxR1 isoform
7.5
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7.5
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the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 7.5
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SwissProt
brenda
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isoform TR1
brenda
isoform TR2
brenda
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TrxR-1(cyto)
brenda
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brenda
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isoform TrxR1
brenda
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brenda
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isoform TrxR3 and TrxR1
brenda
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TrxR-1(mito)
brenda
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TRXR1_DROME
596
0
64322
Swiss-Prot
Mitochondrion (Reliability: 3 )
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53200
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cytosolic TrxR1 isoform, deduced from amino acid sequence
55000
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12% reducing SDS-PAGE
63700
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mitochondrial TrxR1 isoform, deduced from amino acid sequence
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?
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x * 53200, TrxR-1(cyto), calculation from nucleotide sequence
?
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x * 63700, TrxR-1(mito), calculation from nucleotide sequence
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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
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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
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C489S/C490S
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C490S
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
E469A
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the mutant retains 28% of the wild type activity
E469Q
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the mutant retains 35% of the wild type activity
E470A
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the mutant retains 70% of the wild type activity
additional information
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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His-tagged transcript specific mutants, varied N-terminus, 1 null-mutant
additional information
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When the C-terminus of DmTR is changed from a carboxylate to either a thiocarboxylate or a hydroxamic acid, the result is a mutant enzyme with an about 1.7fold increase in activity with thioredoxin. Alanine insertion mutants (DmTR-SCACS and DmTR-SCAACS) show activity with thioredoxin that is greatly reduced compared to that of wild-type DmTR. Increasing the ring size of the Cys-Cys dyad results in a 150-300fold loss in kcat, while the Km is affected little. The 5,5'-dithiobis(2-nitrobenzoic acid) reductase activity of DmTR is also increased when the negative charge at the C-terminus is either neutralized by converting the carboxylate to a neutral hydroxamic acid or modulated by conversion to a thiocarboxylate. Similar to the Sec-containing mammalian enzyme, the truncated DmTR mutant also shows very high 5,5'-dithiobis(2-nitrobenzoic acid) reductase activity, as do the alanine insertion mutants
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DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
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recombinant wild-type cytosolic and mitochondrial isoforms and mutants from Escherichia coli
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expression in Escherichia coli
expressed in Escherichia coli ER2566 cells
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expression of cytosolic and mitochondrial isoform as His-tagged enzymes in Escherichia coli
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wild-type and C-terminal variants
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda