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Literature summary extracted from

  • Juarez, O.; Shea, M.E.; Makhatadze, G.I.; Barquera, B.
    The role and specificity of the catalytic and regulatory cation-binding sites of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae (2011), J. Biol. Chem., 286, 26383-26390.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.1.1 additional information
-
 additional information steady-state and transient kinetics, together with equilibrium binding measurements to define the number of cation-binding sites and characterize their roles in the enzyme, overview Vibrio cholerae serotype O1

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.1.1 membrane
-
 Vibrio cholerae serotype O1 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 K+ acts as a nonessential activator, increasing the activity and affinity for sodium. Na+-NQR contains a regulatory site for K+ Vibrio cholerae serotype O1
7.2.1.1 Li+ stimulates the enzyme Vibrio cholerae serotype O1
7.2.1.1 Na+ stimulates the enzyme Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in Vibrio cholerae serotype O1
-
 NAD+ + ubiquinol + n Na+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio cholerae serotype O1
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
7.2.1.1 reconstitution of Na+-NQR in proteoliposomes and generation of membrane potential. Purified Na+-NQR is mixed with Escherichia coli phospholipids and n-octyl glucoside (detergent/phospholipid ratio = 1.3) in buffer containing 100 mM KCl, 50 mM HEPES, 1 mM EDTA, pH 7.0. The detergent is removed slowly Vibrio cholerae serotype O1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.1 additional information Na+-NQR enables pumping of Li+, as well as Na+ across the membrane, but the enzyme is not able to translocate other monovalent cations, such as potassium or rubidium Vibrio cholerae serotype O1 ?
-
 ?
7.2.1.1 NADH + H+ + ubiquinone + n Li+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol + n Li+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol + n Na+/out
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na+-NQR
-
 Vibrio cholerae serotype O1
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
 Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD noncovalently bound FAD Vibrio cholerae serotype O1
7.2.1.1 FMN covalently bound FMN Vibrio cholerae serotype O1
7.2.1.1 NADH
-
 Vibrio cholerae serotype O1
7.2.1.1 riboflavin noncovalently bound riboflavin Vibrio cholerae serotype O1

General Information

EC Number General Information Comment Organism
7.2.1.1 physiological function the Na+-translocating NADH:quinone oxidoreductase is the entry site for electrons into the respiratory chain and the main sodium pump in Vibrio cholerae Vibrio cholerae serotype O1