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Literature summary for 1.18.1.2 extracted from

  • Catalano-Dupuy, D.L.; Orecchia, M.; Rial, D.V.; Ceccarelli, E.A.
    Reduction of the pea ferredoxin-NADP(H) reductase catalytic efficiency by the structuring of a carboxyl-terminal artificial metal binding site (2006), Biochemistry, 45, 13899-13909.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information addition of an artificial metal binding site of nine amino acids, including four His residues, to the C-terminal Tyr308 residue. The additional structure binds Zn2+ or Co2+ and significantly reduces the catalytic efficiency of the enzyme by decreasing the kcat value. In absence of Zn2+, Km value of NADPH and Kd value for NADP+ are increased 2 to 3 times Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
NADPH wild-type, 30°C, pH 8.0 Pisum sativum
0.0024
-
NADPH mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0 Pisum sativum
0.0026
-
NADPH mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0 Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
-
Pisum sativum NADP+ + reduced 2,6-dichlorophenolindophenol
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2
-
NADPH wild-type, 30°C, pH 8.0 Pisum sativum
10.1
-
NADPH mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0 Pisum sativum
73.5
-
NADPH mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0 Pisum sativum
74.1
-
NADPH wild-type, 30°C, pH 8.0 Pisum sativum