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Literature summary for 7.2.1.1 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
Search for more literature for 7.2.1.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Li+ stimulates the enzyme Vibrio cholerae serotype O1
Na+ stimulates the enzyme Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Vibrio cholerae serotype O1
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
NADH + H+ + ubiquinone + n Li+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol + n Li+/out
-
 ?
NADH + H+ + ubiquinone + n Na+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol + n Na+/out
-
 ?

Synonyms

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

Cofactor

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

General Information

General Information Comment Organism
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