EC Number   |
Protein Variants |
Reference |
|---|
   1.8.7.2 | 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 |
703693 |
| 1.8.7.2 | C57S |
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 |
704409 |
| 1.8.7.2 | 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 |
703693 |
| 1.8.7.2 | C87A |
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 |
704409 |
| 1.8.7.2 | H86Y |
active site mutant, great reduction in activity. Mutant forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S |
704409 |
| 1.8.7.2 | H86Y |
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 |
702253 |
| 1.8.7.2 | more |
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 |
703693 |
| 1.8.7.2 | more |
deletion of the C-terminal tail in GvDTR abolishing enzyme activity |
-, 765599 |
| 1.8.7.2 | more |
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 |
706343 |
| 1.8.7.2 | more |
labeling of cysteinyl residues in the active site by alkylation and spectroscopic analysis, overview |
702192 |
