Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Yano, T.; Yagi, T.
    H+-Translocating NADH-quinone oxidoreductase (NDH-1) of paracoccus denitrificans. Studies on topology and stoichiometry of the peripheral subunits (1999), J. Biol. Chem., 274, 28606-18611.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 cytoplasmic membrane
-
 Paracoccus denitrificans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.2 Iron enzyme complex contains up to 8 iron-sulfur clusters, 2 * [2Fe-2S] and 6 * [4Fe-4S] Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.2 NADH + ubiquinone Paracoccus denitrificans proton-translocating enzyme ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.2 Paracoccus denitrificans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + ubiquinone proton-translocating enzyme Paracoccus denitrificans NAD+ + ubiquinol
-
 ?
7.1.1.2 NADH + ubiquinone proton-translocating enzyme Paracoccus denitrificans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.2 More enzyme is composed of at least 14 subunits Paracoccus denitrificans

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 FMN the enzyme complex contains one molecule of FMN Paracoccus denitrificans
7.1.1.2 NADH
-
 Paracoccus denitrificans