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Literature summary for 1.18.1.3 extracted from

  • Chen, Y.P.; Yoch, D.C.
    Isolation, characterization, and biological activity of ferredoxin-NAD+ reductase from the methane oxidizer Methylosinus trichosporium OB3b (1989), J. Bacteriol., 171, 5012-5016.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-values for transhydrogenase reaction Methylosinus trichosporium OB3b
0.125
-
NADH
-
Methylosinus trichosporium OB3b

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
gel filtration Methylosinus trichosporium OB3b

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxidized ferredoxin + NADH Methylosinus trichosporium OB3b the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin reduced ferredoxin + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Methylosinus trichosporium OB3b
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methylosinus trichosporium OB3b

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.75
-
-
Methylosinus trichosporium OB3b

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme also has transhydrogenase activity which transfers electrons and protons from NADH to thionicotinamide adenine dinucleotide phosphate and from NADPH to acetylpyridine adenine dinucleotide Methylosinus trichosporium OB3b ?
-
?
oxidized ferredoxin + NADH the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin Methylosinus trichosporium OB3b reduced ferredoxin + NAD+
-
?

Cofactor

Cofactor Comment Organism Structure
NADH specific for NADH Methylosinus trichosporium OB3b