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Literature summary for 1.7.7.1 extracted from

  • Hirasawa, M.; Proske, P.A.; Knaff, D.B.
    The role of tryptophan in the reaction catalyzed by spinach ferredoxin-dependent nitrite reductase (1994), Biochim. Biophys. Acta, 1187, 80-88.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
N-bromosuccinimide incubation for 8 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity without effect on substrate binding or other enzyme activities, complex formation with ferredoxin protects the enzyme against inhibition; modifies tryptophane and cysteine residues, incubation for 8 hours with 8-fold excess of NBS leads to 50% inhibition of the catalytic activity, incubation for 16 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Spinacia oleracea 9507
-

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Spinacia oleracea

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
135
-
methyl viologen as electron donor Spinacia oleracea
188
-
ferredoxin as electron donor Spinacia oleracea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover number decreases about 20% after treatment with N-bromosuccinimide Spinacia oleracea