1.8.1.9: thioredoxin-disulfide reductase
This is an abbreviated version!
For detailed information about thioredoxin-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.9
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1.8.1.9
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selenium
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selenoproteins
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selenocysteine
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gsh
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peroxiredoxins
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dismutase
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catalase
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auranofin
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glutaredoxins
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trx1
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selenoenzyme
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hydroperoxide
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peroxidases
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fad
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ribonucleotide
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redox-active
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cisplatin
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dithiols
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goldi
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se-deficient
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dtnb
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iodothyronine
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flavoenzyme
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ebselen
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redox-sensitive
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selenium-containing
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selenols
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deiodinases
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thiol-dependent
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organoselenium
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thioredoxin-like
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selenium-deficient
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se-dependent
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n-heterocyclic
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thioredoxin-dependent
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diselenide
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redox-regulated
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selenium-dependent
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thiol-disulfide
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thiol-based
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thioredoxin-1
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ask1
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carbene
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1-chloro-2,4-dinitrobenzene
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sulforaphane
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secis
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txnip
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trypanothione
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medicine
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analysis
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na2seo3
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agriculture
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thioredoxin-interacting
- 1.8.1.9
- selenium
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selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
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selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
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redox-active
- cisplatin
- dithiols
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goldi
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se-deficient
- dtnb
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iodothyronine
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flavoenzyme
- ebselen
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redox-sensitive
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selenium-containing
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selenols
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deiodinases
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thiol-dependent
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organoselenium
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thioredoxin-like
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selenium-deficient
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se-dependent
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n-heterocyclic
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thioredoxin-dependent
- diselenide
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redox-regulated
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selenium-dependent
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thiol-disulfide
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thiol-based
- thioredoxin-1
- ask1
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carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
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secis
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txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
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thioredoxin-interacting
Reaction
Synonyms
all0737, ApTR, At2g41680, AtNTRA, AtNTRB, bacillithiol disulfide reductase, bacillithiol-disulfide reductase, BBOV_I002190, Bdr, BSSB reductase, CeTR2, DmTR, DmTrxR, DmTrxR-1, EC 1.6.4.5, EhTRXR, ferredoxin:thioredoxin reductase, FTR, general stress protein 35, GSP35, HCOI_01258400, hemolysate thioredoxin reductase, hemolysate TR, hTrxR, HvNTR1, HvNTR2, L-TR, L-TrxR, More, MtNTRC, mTR3, multifunctional thioredoxin-glutathione reductase, NAD(P)H:paraquat oxidoreductase, NADP-dependent thioredoxin reductase, NADP-linked thioredoxin reductase, NADP-thioredoxin reductase, NADP-thioredoxin reductase C, NADPH thioredoxin reductase, NADPH thioredoxin reductase C, NADPH-dependent thioredoxin reductase, NADPH-dependent thioredoxin reductase 2, NADPH-dependent thioredoxin reductase C, NADPH-dependent thioredoxin reductase I, NADPH-dependent thioredoxin reductase-1, NADPH-dependent TRX reductase, NADPH-thioredoxin reductase, NADPH-thioredoxin reductase C, NADPH-Trx reductase, NADPH2:oxidized thioredoxin oxidoreductase, NAPDH-dependent BSSB reductase, NTR, Ntr1, NTR2, Ntr3, NTRA, NTRAB, NtrB, NTRC, PH0178, PH1426, PhRP, PhTrxR, protein-disulfide oxidoreductase, reductase, thioredoxin, SEP1, taTrxR, TGR, thioredoxin glutathione reductase, thioredoxin h reductase, thioredoxin reductase, thioredoxin reductase (NADPH), thioredoxin reductase 1, thioredoxin reductase 2, thioredoxin reductase-1, thioredoxin reductase1, TON_1603, TR, TR1, TR2, TR3, TRase, TrR, Trr1, Trr1p, TRR2, Trx1, Trx3, TrxB, TrxB1, TrxB2, TrxR, TrxR-1(cyto), TrxR-1(mito), TrxR1, TrxR2, TrxR3, TrxRB3, TRXRD, TrxRh1, TrxRh2, TrxT, Txnrd1, TXNRD1-v3, Txnrd2, TXNRD3, TxrR-1, YpdA
ECTree
1.8.1.9 thioredoxin-disulfide reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.8.1.9 - thioredoxin-disulfide reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C142A
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mutant shows reduced reductase activity compared to the wild type enzyme
C142S
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mutant shows reduced reductase activity compared to the wild type enzyme
C145A
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mutant shows reduced reductase activity compared to the wild type enzyme
C145S
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mutant shows reduced reductase activity compared to the wild type enzyme
A164G/R183F
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the mutant shows reduced activity but is still able to dimerize though with an increase in intermediary forms
A164G/V182E
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the mutant shows increased activity compared to the wild type enzyme
A164G/V182E/R183F
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the mutant shows reduced activity compared to the wild type enzyme but is still able to dimerize though with an increase in intermediary forms
C120A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C122A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C120A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C120A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C122A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A/C120A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A/C220A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C220A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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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
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
C135S
C135S/C32S
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via the active disulfide centers a subunit complex of tightly bound enzyme, C135 and C138, and thioredoxin, C32 and C35, is formed, exchange of one cysteine for one serine in each protein by site-directed mutagenesis, conformation analysis
C135S/C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C138S
C138S/C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C32S
C35S
TrxR-16
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truncated form of TrxR missing the last 16 C-terminal amino acids, without thioredoxin-reducing activity
C148S
residue Cys148 probably performs an initial nucleophilic attack on the active site disulfide in thioredoxin disulfide. Kinetic data
M43A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin. Kinetic data
W42A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin. Kinetic data
W42A/M43A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin
U489C
barely detectable activity towards thioredoxin and hydrogen peroxide
C535S
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construction of a homodimer and heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 56 and 92%, respectively
C535S/C88A
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double mutant, construction of a homodimer and a heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 89 and 95%, respectively
C88A
C146S
no activity against insulin disulfide, no DTNB-reducing activity
C35S
strong activity as high as that of a wild type against insulin disulfide, 98% of residual activity. The activity of C35S against the reduction of DTNB was not decreased
C35S
Pyrococcus furiosus OT-3
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strong activity as high as that of a wild type against insulin disulfide, 98% of residual activity. The activity of C35S against the reduction of DTNB was not decreased
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SCCS
mutant with flanking serine residues introduced into the C-terminal tetrapeptide of the wild type enzyme, less than 0.5% activity of the wild type enzyme
SeC498C
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antisense technique, exchange in the catalytic active selenosulfide at the C-terminus, resulting in higher pH-optimum, 100fold lower turnover number, 10fold lower Km-value, no activity with H2O2
Y116I
C147A
G10A
C57S
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inactive mutant containing a redox-active [Fe4S4]3+/2+ center, can be reduced by dithionite
C53S
site-directed mutagenesis, no activity since the redox cycle system is abolished
additional information
C135S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C135S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 138 is remaining
C138S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C138S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 135 is remaining, very low activity
C32S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C32S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 35 is remaining, low activity
C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C35S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 32 is remaining
C88A
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construction of a homodimer and a heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 4 and 90%
Y116I
the mutation decreases sensitivity to inhibition by cisplatin and lowers catalytic efficiency in reduction of thioredoxin compared to the wild type enzyme
Y116I
the mutation decreases sensitivity to inhibition by cisplatin, lowers catalytic efficiency in reduction of thioredoxin, and increases turnover using 5-hydroxy-1,4-naphthoquinone (juglone) as substrate compared to the wild type enzyme
C147A
significantly reduced activity, decrease in FAD content
C147A
the mutant exhibits a marginal NADH oxidase activity with FAD canonically bound to the enzyme
C147A
in the active site of the C147A mutant, which exhibits a marginal NADH oxidase activity, the FAD is canonically bound to the enzyme
G10A
site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
G10A
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site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
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G10A
Staphylococcus aureus PS 47
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site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
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additional information
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where insertion of alanine between the redox-active Cys residues of the C-terminal redox center has very little effect on DTNB reductase activity
additional information
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His-tagged transcript specific mutants, varied N-terminus, 1 null-mutant
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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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
additional information
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trxB gene is combined to chimeric enzyme NT-TrR by exchanging the N-terminus of Escherichia coli with the N-terminus of Salmonella typhimurium AhpF gene protein, which encodes a protein with about 35% homology in the N-terminal region, 2 other mutants are constructed in the same way but with double mutation C129S/C132S and C342S/C345S, the first in the Escherichia coli part and the latter in the Salmonella part of the chimeric protein, activity corressponding to organism wild-type giving the N-terminal part, except for C342S/C345S chimeric mutant who has no activity
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
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expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
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the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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thioredoxin is cut off the native fusion protein thioredoxin-thioredoxin reductase resulting in enhanced activity
additional information
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truncated enzyme mutant without catalytic active C-terminus
additional information
mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
additional information
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mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
additional information
-
mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
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additional information
Staphylococcus aureus PS 47
-
mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
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