1.8.7.2: ferredoxin:thioredoxin reductase
This is an abbreviated version!
For detailed information about ferredoxin:thioredoxin reductase, go to the full flat file.
Word Map on EC 1.8.7.2
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1.8.7.2
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thioredoxins
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chloroplast
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spinach
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redox-active
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reductases
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epr
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fe-s
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light-dependent
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one-electron-reduced
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two-electron
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iron-sulfur
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raman
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one-electron
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variable-temperature
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heterodisulfide
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dithiol
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methanosarcina
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synthesis
- 1.8.7.2
- thioredoxins
- chloroplast
- spinach
-
redox-active
- reductases
- epr
- fe-s
-
light-dependent
-
one-electron-reduced
-
two-electron
-
iron-sulfur
-
raman
-
one-electron
-
variable-temperature
-
heterodisulfide
- dithiol
-
methanosarcina
- synthesis
Reaction
2 reduced ferredoxin
+
Synonyms
Fd-thioredoxin reductase, Fd:TRX reductase, FdR, Fdx flavin-thioredoxin reductase, Fdx-dependent thioredoxin reductase, FDX-dependent TRX reductase, ferredoxin disulfide reductase, ferredoxin-dependent thioredoxin reductase, ferredoxin-thioredoxin reductase, FFTR, FTR, FTRc, glr0719, GvDTR, iron-sulfur ferredoxin-dependent thioredoxin reductase, Ma_1659, protein modulase
ECTree
1.8.7.2 ferredoxin:thioredoxin reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.8.7.2 - ferredoxin:thioredoxin reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C27S
mutation in truncated, stabilized FTR mutant lacking 24 N-terminal amino acids. Mutant C27S is perfectly capable of activating FBPase and shows a thioredoxin f-concentration dependency comparable to the FTR truncation mutant
C84S
mutation in truncated, stabilized FTR mutant lacking 24 N-terminal amino acids. Mutant C84S is produced at about the same level as the WT protein, it is extremely labile and disintegrates very rapidly during the first steps of purifiation
C57S
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active site mutant, inactive. Spectral analysis indicates a reduced Fe-S cluster which can be reduced by dithionite. Stable protein, forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S
C87A
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active site mutant, inactive. Spectral analysis indicates an oxidized Fe-S cluster. Mutants is unable to form stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S
H86Y
additional information
H86Y
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active site mutant, great reduction in activity. Mutant forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S
H86Y
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spectroscopic and redox characterization of the [Fe4-S4] center in H86Y ferredoxin:thoredoxin reductase in the accessible redox states of both the native and N-ethylmaleimide-modified forms. H86 is required for formation of the partially valence-localized [Fe4-S4]2+ cluster that is the hallmark of two-electron-reduced intermediate. Results indicate a functional role for H86 in protonation/deprotonation of the cluster-interacting thiol and anchoring the cluster interacting thiol in close proximity to the cluster in the two-electron-reduced intermediate
additional information
deletion of the C-terminal tail in GvDTR abolishing enzyme activity
additional information
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deletion of the C-terminal tail in GvDTR abolishing enzyme activity
additional information
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deletion of the C-terminal tail in GvDTR abolishing enzyme activity
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additional information
construction two N-terminal truncation mutants by removing 16 or 24 residues from the variable subunit. The mutant proteins are readily expressed and show half-saturation values for ferredoxin and thioredoxin f comparable to wild-type. Truncation increases significantly their stability
additional information
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construction two N-terminal truncation mutants by removing 16 or 24 residues from the variable subunit. The mutant proteins are readily expressed and show half-saturation values for ferredoxin and thioredoxin f comparable to wild-type. Truncation increases significantly their stability
additional information
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dicistronic construct for the heterologous expression in Escherichia coli. The coding sequences for the two mature subunits have been inserted in tandem into the expression vector. The dicistronic construct is correctly translated yielding soluble, perfectly functional FTR. The recombinant enzyme is composed of both subunits, contains the correctly inserted FeS cluster and is indistinguishable from the enzyme isolated from leaves in its capacity to activate chloroplast fructose-1,6-bisphosphatase
additional information
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labeling of cysteinyl residues in the active site by alkylation and spectroscopic analysis, overview
additional information
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modification of the redox-active disulfide in the active site and of other cysteinyl residues, FTR is incubated for 20 rnin at 25°C with 2 mM N-ethylmaleimide or [l4C]N-ethylmaleimide in 100 mM sodium phosphate, pH 7.0, for the modification of the accessible cysteines and additionally in the presence of 2% SDS for the inaccessible cysteines
additional information
modification of the redox-active disulfide in the active site and of other cysteinyl residues, FTR is incubated for 20 rnin at 25°C with 2 mM N-ethylmaleimide or [l4C]N-ethylmaleimide in 100 mM sodium phosphate, pH 7.0, for the modification of the accessible cysteines and additionally in the presence of 2% SDS for the inaccessible cysteines
