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Literature summary extracted from
- Catalytic properties of Na+-translocating NADH:quinone oxidoreductases from Vibrio harveyi, Klebsiella pneumoniae, and Azotobacter vinelandii (2008), FEMS Microbiol. Lett., 279, 116-123.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.1.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide | inhibited by micromolar concentrations. In contrast to the corresponding enzymes from Vibrio harveyi and Klebsiella pneumoniae, the enzyme from Azotobacter vinelandii is resistant to low 2-n-heptyl-4-hydroxyquinoline N-oxide concentrations | Azotobacter vinelandii |  |
| 7.2.1.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide | - |
Klebsiella pneumoniae | |
| 7.2.1.1 | 2-n-heptyl-4-hydroxyquinoline N-oxide | submicromolar concentrations inhibit | Vibrio harveyi | |
| 7.2.1.1 | Ag+ | 0.001 mM, partial and very slow inhibition | Azotobacter vinelandii | |
| 7.2.1.1 | Ag+ | - |
Vibrio harveyi | |
| 7.2.1.1 | diphenyliodonium | modifies the noncovalently bound FAD of the enzyme | Azotobacter vinelandii | |
| 7.2.1.1 | diphenyliodonium | modifies the noncovalently bound FAD of the enzyme | Klebsiella pneumoniae | |
| 7.2.1.1 | diphenyliodonium | 0.05 mM, rapid inhibition, modifies the noncovalently bound FAD of the enzyme | Vibrio harveyi | |
| 7.2.1.1 | additional information | the enzyme is fully resistant to either Ag+ or N-ethylmaleimide | Azotobacter vinelandii | |
| 7.2.1.1 | additional information | the enzyme is fully resistant to either Ag+ or N-ethylmaleimide | Klebsiella pneumoniae | |
| 7.2.1.1 | NEM | 5 mM, inhibits partially and very slowly | Azotobacter vinelandii | |
| 7.2.1.1 | NEM | 5 mM, rapid inhibition | Vibrio harveyi | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.1.1 | additional information | - |
additional information | Km(Na+) is 0.0001 mM | Azotobacter vinelandii | |
| 7.2.1.1 | additional information | - |
additional information | Km(Na+) is 0.067 mM | Klebsiella pneumoniae | |
| 7.2.1.1 | additional information | - |
additional information | Km(Na+) is 0.67 mM | 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 | Klebsiella pneumoniae | construction of a double NDH-2/NDH-1-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes | ? | - |
? | |
| 7.2.1.1 | additional information | Vibrio harveyi | construction of a NADH-dehydrogenase NDH-2-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.2.1.1 | Azotobacter vinelandii | - |
- |
- |
| 7.2.1.1 | Klebsiella pneumoniae | - |
- |
- |
| 7.2.1.1 | Vibrio harveyi | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.2.1.1 | - |
Vibrio harveyi |
| 7.2.1.1 | - |
Klebsiella pneumoniae |
| 7.2.1.1 | - |
Azotobacter vinelandii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.1.1 | additional information | construction of a double NDH-2/NDH-1-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes | Klebsiella pneumoniae | ? | - |
? | |
| 7.2.1.1 | additional information | construction of a NADH-dehydrogenase NDH-2-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes | Vibrio harveyi | ? | - |
? | |
| 7.2.1.1 | additional information | Na+-translocating NADH:quinone oxidoreductases activity, the enzyme also shows NADH-oxidase activity | Azotobacter vinelandii | ? | - |
? | |
| 7.2.1.1 | additional information | the enzyme also shows NADH-oxidase activity | Vibrio harveyi | ? | - |
? | |
| 7.2.1.1 | additional information | the enzyme also shows NADH-oxidase activity | Klebsiella pneumoniae | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.1.1 | Na+-translocating NADH:quinone oxidoreductase | - |
Klebsiella pneumoniae |
| 7.2.1.1 | Na+-translocating NADH:quinone oxidoreductase | - |
Azotobacter vinelandii |
| 7.2.1.1 | Na+-translocatingNADH:quinone oxidoreductase | - |
Vibrio harveyi |
| 7.2.1.1 | Na1-NQR | - |
Vibrio harveyi |
| 7.2.1.1 | Na1-NQR | - |
Klebsiella pneumoniae |
| 7.2.1.1 | Na1-NQR | - |
Azotobacter vinelandii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.1.1 | NADH | no activity with NADPH | Vibrio harveyi | |
| 7.2.1.1 | NADH | no activity with NADPH | Klebsiella pneumoniae | |
| 7.2.1.1 | NADH | no activity with NADPH | Azotobacter vinelandii | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 7.2.1.1 | 0.0001 | - |
- |
Vibrio harveyi | Ag+ | |
| 7.2.1.1 | 0.00013 | - |
- |
Vibrio harveyi | 2-n-heptyl-4-hydroxyquinoline N-oxide | |
| 7.2.1.1 | 0.00055 | - |
- |
Klebsiella pneumoniae | 2-n-heptyl-4-hydroxyquinoline N-oxide | |
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