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Literature summary for 1.7.7.1 extracted from

  • Hirasawa, M.; de Best, J.H.; Knaff, D.B.
    The effect of lysine- and arginine-modifying reagents on spinach ferredoxin:nitrite oxidoreductase (1993), Biochim. Biophys. Acta, 1140, 304-312.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
N-acetylsuccinimide loss of enzymatic activity when reduced ferredoxin serves as electron donor, but very little effect with methyl viologen as electron donor, ferredoxin protects the enzyme Spinacia oleracea
Phenylglyoxal loss of enzymatic activity when reduced ferredoxin serves as electron donor, but very little effect with methyl viologen as electron donor, ferredoxin protects the enzyme Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
methyl viologen
-
Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
SDS-PAGE Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
spinach
-

Purification (Commentary)

Purification (Comment) Organism
-
Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
90
-
methyl viologen as electron donor Spinacia oleracea
120
-
ferredoxin as electron donor Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + reduced methyl viologen
-
Spinacia oleracea NH3 + H2O + oxidized methyl viologen
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
-
Spinacia oleracea