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Literature summary for 1.18.1.1 extracted from

  • Ueda, T.; Coon, M.J.
    Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation (1972), J. Biol. Chem., 247, 5010-5016.
    View publication on PubMed
Search for more literature for 1.18.1.1

Inhibitors

Inhibitors Comment Organism Structure
AgNO3
-
 Pseudomonas oleovorans
NAD+
-
 Pseudomonas oleovorans
NADPH
-
 Pseudomonas oleovorans
p-mercuribenzoate
-
 Pseudomonas oleovorans
Sodium mersalyl
-
 Pseudomonas oleovorans
Tetrodotoxin
-
 Pseudomonas oleovorans
thionicotinamide-NAD+
-
 Pseudomonas oleovorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + oxidized rubredoxin Pseudomonas oleovorans enzyme is required for fatty acid and alkane hydroxylation NAD+ + reduced rubredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas oleovorans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Pseudomonas oleovorans 2 ferrocyanide + NAD+ + H+
-
 ?
additional information no activity with spinach ferredoxin, putidaredoxin and adrenodoxin Pseudomonas oleovorans ?
-
 ?
additional information enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH Pseudomonas oleovorans ?
-
 ?
NADH + 2,6-dichloroindophenol
-
 Pseudomonas oleovorans NAD+ + reduced 2,6-dichloroindophenol
-
 ?
NADH + oxidized rubredoxin enzyme catalyzes electron transfer not only to the rubredoxin of Pseudomonas oleovorans but also to the lower molecular weight rubredoxins of the anaerobic bacteria Peptostreptococcus elsdenii, Clostridium pasteurianum and Desulfovibrio gigas Pseudomonas oleovorans NAD+ + reduced rubredoxin
-
 ?
NADH + oxidized rubredoxin enzyme is required for fatty acid and alkane hydroxylation Pseudomonas oleovorans NAD+ + reduced rubredoxin
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol per mol of enzyme Pseudomonas oleovorans
NADH NADH is highly superior to NADPH as electron donor Pseudomonas oleovorans
NADPH NADH is highly superior to NADPH as electron donor Pseudomonas oleovorans