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Literature summary for 7.2.1.1 extracted from

  • Tao, M.; Casutt, M.S.; Fritz, G.; Steuber, J.
    Oxidant-induced formation of a neutral flavosemiquinone in the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae (2008), Biochim. Biophys. Acta, 1777, 696-702.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Vibrio cholerae serotype O1

Inhibitors

Inhibitors Comment Organism Structure
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
Vibrio cholerae serotype O1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21470
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
22837
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
27619
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
45067
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
45357
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
48624
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
110000
-
NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, gel filtration Vibrio cholerae serotype O1
306000
-
one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50–76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, gel filtration Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + ubiquinone-1 Vibrio cholerae serotype O1 the enzyme catalyzes NADH-driven Na+ transport NAD+ + ubiquinol-1
-
?
NADH + H+ + ubiquinone-1 Vibrio cholerae serotype O1 ATCC 39315 the enzyme catalyzes NADH-driven Na+ transport NAD+ + ubiquinol-1
-
?

Organism

Organism UniProt Comment Textmining
Vibrio cholerae serotype O1 Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
-
Vibrio cholerae serotype O1 ATCC 39315 Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Vibrio cholerae serotype O1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H+ + ubiquinone-1
-
Vibrio cholerae serotype O1 NAD+ + ubiquinol-1
-
?
NADH + H+ + ubiquinone-1 the enzyme catalyzes NADH-driven Na+ transport Vibrio cholerae serotype O1 NAD+ + ubiquinol-1
-
?
NADH + H+ + ubiquinone-1
-
Vibrio cholerae serotype O1 ATCC 39315 NAD+ + ubiquinol-1
-
?
NADH + H+ + ubiquinone-1 the enzyme catalyzes NADH-driven Na+ transport Vibrio cholerae serotype O1 ATCC 39315 NAD+ + ubiquinol-1
-
?

Subunits

Subunits Comment Organism
hexamer 1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence Vibrio cholerae serotype O1
tetramer 1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence Vibrio cholerae serotype O1

Synonyms

Synonyms Comment Organism
Na+-NQR
-
Vibrio cholerae serotype O1
Na+-translocating NADH:quinone oxidoreductase
-
Vibrio cholerae serotype O1
NADH:quinone oxidoreductase
-
Vibrio cholerae serotype O1
NQR-1 complex which elutes at an approximate molecular mass of 306 kDa is termed NQR-1. One copy of each Nqr subunit is present in the Na+-NQR (NqrA-His, NqrF, NqrB, NqrC, NqrD and NqrE). NQR-1 mainly consists of monomeric Na+-NQR Vibrio cholerae serotype O1
NQR-2 the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunits Vibrio cholerae serotype O1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Vibrio cholerae serotype O1

Cofactor

Cofactor Comment Organism Structure
FAD the isolated enzyme complex contains near-stoichiometric amounts of non-covalently bound FAD (0.78 mol/mol Na+-NQR) and riboflavin (0.70 mol/mol Na+-NQR). The four flavins in the Na+-NQR are converted to the partially or fully reduced state when the enzyme reacts with NADH. Two non-covalently bound flavins (FAD and riboflavin) preferentially act as two-electron mediators, whereas two covalently bound FMNs undergo one-electron transitions (FMN/FMNU(radical)-) Vibrio cholerae serotype O1
FMN four flavins in the Na+-NQR are converted to the partially or fully reduced state when the enzyme reacts with NADH. Two non-covalently bound flavins (FAD and riboflavin) preferentially act as two-electron mediators, whereas two covalently bound FMNs undergo one-electron transitions (FMN/FMNU(radical)-) Vibrio cholerae serotype O1
NADH
-
Vibrio cholerae serotype O1
NADH NQR-2 exhibits approximately 15% of the specific NADH dehydrogenase activity of NQR-1 Vibrio cholerae serotype O1
riboflavin riboflavin detected in NQR-2 is bound to the NqrB or NqrC subunit Vibrio cholerae serotype O1
riboflavin the isolated enzyme complex contains near-stoichiometric amounts of non-covalently bound FAD (0.78 mol/mol Na+-NQR) and riboflavin (0.70 mol/mol Na+-NQR). The four flavins in the Na+-NQR are converted to the partially or fully reduced state when the enzyme reacts with NADH. Two non-covalently bound flavins (FAD and riboflavin) preferentially act as two-electron mediators, whereas two covalently bound FMNs undergo one-electron transitions (FMN/FMNU(radical)-) Vibrio cholerae serotype O1