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Literature summary for 1.7.1.14 extracted from

  • Daiber, A.; Shoun, H.; Ullrich, V.
    Nitric oxide reductase (P450nor) from Fusarium oxysporum (2005), J. Inorg. Biochem., 99, 185-193.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
gel filtration Fusarium oxysporum

Organism

Organism UniProt Comment Textmining
Fusarium oxysporum
-
-
-
Fusarium oxysporum MT-811
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is peculiar in requiring only NADH and no electron transport system for the reduction of NO. NADPH is much less active as the cosubstrate Fusarium oxysporum ?
-
?
additional information the enzyme is peculiar in requiring only NADH and no electron transport system for the reduction of NO. NADPH is much less active as the cosubstrate Fusarium oxysporum MT-811 ?
-
?
NO + NAD(P)H + H+
-
Fusarium oxysporum N2O + NAD(P)+ + H2O
-
?
NO + NAD(P)H + H+
-
Fusarium oxysporum MT-811 N2O + NAD(P)+ + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 46000, SDS-PAGE Fusarium oxysporum

Synonyms

Synonyms Comment Organism
cytochrome P450 NADH-NO reductase
-
Fusarium oxysporum
P450nor
-
Fusarium oxysporum

Cofactor

Cofactor Comment Organism Structure
heme the enzyme is a heme-thiolate protein Fusarium oxysporum
NADH
-
Fusarium oxysporum
NADPH NADPH is much less active as the cosubstrate than NADH Fusarium oxysporum

General Information

General Information Comment Organism
physiological function P450nor has an important role in protecting the fungus from NO inhibition of mitochondria especially when dioxygen becomes limiting Fusarium oxysporum