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Literature summary for 1.14.12.17 extracted from

  • Gardner, P.R.; Gardner, A.M.; Martin, L.A.; Salzman, A.L.
    Nitric oxide dioxygenase: an enzymic function for flavohemoglobin (1998), Proc. Natl. Acad. Sci. USA, 95, 10378-10383.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
hemin maximal activity at 0.001 mM Escherichia coli

General Stability

General Stability Organism
stabilizing of activity during gel filtration by adding 10 mM NaN3 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NaCN 45% of control activity with 0.025 mM, 2% with 0.25 mM Escherichia coli
Superoxide dismutase
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.015
-
strain AB1157 Escherichia coli
0.865
-
mutant strain PG118 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NO + O2 + NAD(P)H
-
Escherichia coli NO3- + NAD(P)+ + H+
-
?

Cofactor

Cofactor Comment Organism Structure
FAD full activity at 0.001 mM Escherichia coli
NADPH
-
Escherichia coli
O2
-
Escherichia coli