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Literature summary extracted from

  • Aliverti, A.; Jansen, T.; Zanetti, G.; Ronchi, S.; Herrmann, R.G.; Curti, B.
    Expression in Escherichia coli of ferredoxin:NADP+ reductase from spinach. Bacterial synthesis of the holoflavoprotein and of an active enzyme form lacking the first 28 amino acid residues of the sequence (1990), Eur. J. Biochem., 191, 551-555.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.2 two forms, one lacks the first 28 amino acid residues, has full diaphorase activity but reduced NADPH/cytochrome-c activity Spinacia oleracea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 0.049
-
Ferredoxin 35 kDa enzyme Spinacia oleracea
1.18.1.2 0.053
-
Ferredoxin 32 kDa enzyme Spinacia oleracea

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.2 32000
-
lack of the first 28 amino acid residues after expression in Escherichia coli Spinacia oleracea
1.18.1.2 35000
-
after expression in E. coli Spinacia oleracea

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Spinacia oleracea
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.18.1.2 76
-
diaphorase activity of the 32 kDa enzyme Spinacia oleracea
1.18.1.2 79
-
diaphorase activity of the 35 kDa enzyme Spinacia oleracea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+
-
Spinacia oleracea oxidized ferredoxin + NADPH + H+
-
r