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Literature summary for 1.8.7.2 extracted from

  • Manieri, W.; Franchini, L.; Raeber, L.; Dai, S.; Stritt-Etter, A.L.; Schurmann, P.
    N-terminal truncation of the variable subunit stabilizes spinach ferredoxin:thioredoxin reductase (2003), FEBS Lett., 549, 167-170.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
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 Spinacia oleracea
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 Spinacia oleracea
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 Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea P38365 variable subunit
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