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Literature summary extracted from

  • Bogachev, A.V.; Verkhovsky, M.I.
    Na+-translocating NADH:quinone oxidoreductase: progress achieved and prospects of investigations (2005), Biochemistry, 70, 143-149.
    View publication on PubMed

Application

EC Number Application Comment Organism
7.2.1.1 medicine Vibrio cholerae Na+-NQR is significant for the induction of virulence factors. Thus, this enzyme can be used as a target in the treatment or prevention of many infectious diseases Vibrio cholerae serotype O1

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Haemophilus influenzae
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Klebsiella pneumoniae
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Neisseria gonorrhoeae
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Neisseria meningitidis
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Porphyromonas gingivalis
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Pseudomonas aeruginosa
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Shewanella putrefaciens
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Vibrio alginolyticus
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Vibrio cholerae serotype O1
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Vibrio harveyi
7.2.1.1 2-heptyl-4-hydroxyquinoline N-oxide
-
Yersinia pestis
7.2.1.1 korormicin
-
Haemophilus influenzae
7.2.1.1 korormicin
-
Klebsiella pneumoniae
7.2.1.1 korormicin
-
Neisseria gonorrhoeae
7.2.1.1 korormicin
-
Neisseria meningitidis
7.2.1.1 korormicin
-
Porphyromonas gingivalis
7.2.1.1 korormicin
-
Pseudomonas aeruginosa
7.2.1.1 korormicin
-
Shewanella putrefaciens
7.2.1.1 korormicin
-
Vibrio alginolyticus
7.2.1.1 korormicin
-
Vibrio cholerae serotype O1
7.2.1.1 korormicin
-
Vibrio harveyi
7.2.1.1 korormicin
-
Yersinia pestis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Haemophilus influenzae
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Vibrio harveyi
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Pseudomonas aeruginosa
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Neisseria gonorrhoeae
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Neisseria meningitidis
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Klebsiella pneumoniae
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Yersinia pestis
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Porphyromonas gingivalis
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Vibrio cholerae serotype O1
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Vibrio alginolyticus
7.2.1.1 Na+ sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion Shewanella putrefaciens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.2.1.1 21500
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi
7.2.1.1 22700
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi
7.2.1.1 27500
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi
7.2.1.1 45200
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi
7.2.1.1 45400
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi
7.2.1.1 48400
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.1.1 additional information Porphyromonas gingivalis in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinines. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Vibrio harveyi in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Vibrio alginolyticus in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Haemophilus influenzae in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Pseudomonas aeruginosa in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Neisseria gonorrhoeae in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Neisseria meningitidis in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Klebsiella pneumoniae in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Yersinia pestis in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Vibrio cholerae serotype O1 in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 additional information Shewanella putrefaciens in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin ?
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Haemophilus influenzae
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Vibrio harveyi
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Pseudomonas aeruginosa
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Neisseria gonorrhoeae
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Neisseria meningitidis
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Klebsiella pneumoniae
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Yersinia pestis
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Porphyromonas gingivalis
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Vibrio cholerae serotype O1
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Vibrio alginolyticus
-
NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in Shewanella putrefaciens
-
NAD+ + ubiquinol + 2 Na+/out
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Haemophilus influenzae
-
-
-
7.2.1.1 Klebsiella pneumoniae
-
-
-
7.2.1.1 Neisseria gonorrhoeae
-
-
-
7.2.1.1 Neisseria meningitidis
-
-
-
7.2.1.1 Porphyromonas gingivalis
-
-
-
7.2.1.1 Pseudomonas aeruginosa
-
-
-
7.2.1.1 Shewanella putrefaciens
-
-
-
7.2.1.1 Vibrio alginolyticus
-
-
-
7.2.1.1 Vibrio cholerae serotype O1
-
-
-
7.2.1.1 Vibrio harveyi
-
-
-
7.2.1.1 Yersinia pestis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinines. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Porphyromonas gingivalis ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Vibrio harveyi ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Vibrio alginolyticus ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Haemophilus influenzae ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Pseudomonas aeruginosa ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Neisseria gonorrhoeae ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Neisseria meningitidis ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Klebsiella pneumoniae ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Yersinia pestis ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Vibrio cholerae serotype O1 ?
-
?
7.2.1.1 additional information in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin Shewanella putrefaciens ?
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Haemophilus influenzae NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Vibrio harveyi NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Pseudomonas aeruginosa NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Neisseria gonorrhoeae NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Neisseria meningitidis NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Klebsiella pneumoniae NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Yersinia pestis NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Porphyromonas gingivalis NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Vibrio cholerae serotype O1 NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Vibrio alginolyticus NAD+ + ubiquinol + 2 Na+/out
-
?
7.2.1.1 NADH + H+ + ubiquinone + 2 Na+/in
-
Shewanella putrefaciens NAD+ + ubiquinol + 2 Na+/out
-
?

Subunits

EC Number Subunits Comment Organism
7.2.1.1 heterohexamer
-
Haemophilus influenzae
7.2.1.1 heterohexamer
-
Pseudomonas aeruginosa
7.2.1.1 heterohexamer
-
Neisseria gonorrhoeae
7.2.1.1 heterohexamer
-
Neisseria meningitidis
7.2.1.1 heterohexamer
-
Klebsiella pneumoniae
7.2.1.1 heterohexamer
-
Yersinia pestis
7.2.1.1 heterohexamer
-
Porphyromonas gingivalis
7.2.1.1 heterohexamer
-
Vibrio cholerae serotype O1
7.2.1.1 heterohexamer
-
Vibrio alginolyticus
7.2.1.1 heterohexamer
-
Shewanella putrefaciens
7.2.1.1 heterohexamer 1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200 Vibrio harveyi

Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na+-NQR
-
Haemophilus influenzae
7.2.1.1 Na+-NQR
-
Vibrio harveyi
7.2.1.1 Na+-NQR
-
Pseudomonas aeruginosa
7.2.1.1 Na+-NQR
-
Neisseria gonorrhoeae
7.2.1.1 Na+-NQR
-
Neisseria meningitidis
7.2.1.1 Na+-NQR
-
Klebsiella pneumoniae
7.2.1.1 Na+-NQR
-
Yersinia pestis
7.2.1.1 Na+-NQR
-
Porphyromonas gingivalis
7.2.1.1 Na+-NQR
-
Vibrio cholerae serotype O1
7.2.1.1 Na+-NQR
-
Vibrio alginolyticus
7.2.1.1 Na+-NQR
-
Shewanella putrefaciens
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Haemophilus influenzae
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Vibrio harveyi
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Pseudomonas aeruginosa
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Neisseria gonorrhoeae
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Neisseria meningitidis
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Klebsiella pneumoniae
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Yersinia pestis
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Porphyromonas gingivalis
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Vibrio cholerae serotype O1
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Vibrio alginolyticus
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
Shewanella putrefaciens

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD noncovalently bound to subunit NqrF Haemophilus influenzae
7.2.1.1 FAD noncovalently bound to subunit NqrF Vibrio harveyi
7.2.1.1 FAD noncovalently bound to subunit NqrF Pseudomonas aeruginosa
7.2.1.1 FAD noncovalently bound to subunit NqrF Neisseria gonorrhoeae
7.2.1.1 FAD noncovalently bound to subunit NqrF Neisseria meningitidis
7.2.1.1 FAD noncovalently bound to subunit NqrF Klebsiella pneumoniae
7.2.1.1 FAD noncovalently bound to subunit NqrF Yersinia pestis
7.2.1.1 FAD noncovalently bound to subunit NqrF Porphyromonas gingivalis
7.2.1.1 FAD noncovalently bound to subunit NqrF Vibrio cholerae serotype O1
7.2.1.1 FAD noncovalently bound to subunit NqrF Vibrio alginolyticus
7.2.1.1 FAD noncovalently bound to subunit NqrF Shewanella putrefaciens
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Haemophilus influenzae
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Vibrio harveyi
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Pseudomonas aeruginosa
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Neisseria gonorrhoeae
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Neisseria meningitidis
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Klebsiella pneumoniae
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Yersinia pestis
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Porphyromonas gingivalis
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Vibrio cholerae serotype O1
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Vibrio alginolyticus
7.2.1.1 FMN covalently bound to subunits NqrB and NqrC Shewanella putrefaciens
7.2.1.1 NADH
-
Haemophilus influenzae
7.2.1.1 NADH
-
Vibrio harveyi
7.2.1.1 NADH
-
Pseudomonas aeruginosa
7.2.1.1 NADH
-
Neisseria gonorrhoeae
7.2.1.1 NADH
-
Neisseria meningitidis
7.2.1.1 NADH
-
Klebsiella pneumoniae
7.2.1.1 NADH
-
Yersinia pestis
7.2.1.1 NADH
-
Porphyromonas gingivalis
7.2.1.1 NADH
-
Vibrio cholerae serotype O1
7.2.1.1 NADH
-
Vibrio alginolyticus
7.2.1.1 NADH
-
Shewanella putrefaciens
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Haemophilus influenzae
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Vibrio harveyi
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Pseudomonas aeruginosa
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Neisseria gonorrhoeae
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Neisseria meningitidis
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Klebsiella pneumoniae
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Yersinia pestis
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Porphyromonas gingivalis
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Vibrio cholerae serotype O1
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Vibrio alginolyticus
7.2.1.1 riboflavin contains a noncovalently bound riboflavin Shewanella putrefaciens
7.2.1.1 ubiquinone-8
-
Haemophilus influenzae
7.2.1.1 ubiquinone-8
-
Vibrio harveyi
7.2.1.1 ubiquinone-8
-
Pseudomonas aeruginosa
7.2.1.1 ubiquinone-8
-
Neisseria gonorrhoeae
7.2.1.1 ubiquinone-8
-
Neisseria meningitidis
7.2.1.1 ubiquinone-8
-
Klebsiella pneumoniae
7.2.1.1 ubiquinone-8
-
Yersinia pestis
7.2.1.1 ubiquinone-8
-
Porphyromonas gingivalis
7.2.1.1 ubiquinone-8
-
Vibrio cholerae serotype O1
7.2.1.1 ubiquinone-8
-
Vibrio alginolyticus
7.2.1.1 ubiquinone-8
-
Shewanella putrefaciens
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Haemophilus influenzae
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Vibrio harveyi
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Pseudomonas aeruginosa
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Neisseria gonorrhoeae
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Neisseria meningitidis
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Klebsiella pneumoniae
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Yersinia pestis
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Porphyromonas gingivalis
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Vibrio cholerae serotype O1
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Vibrio alginolyticus
7.2.1.1 [2Fe-2S]-center part of subunit NqrF Shewanella putrefaciens