1.6.5.9: NADH:quinone reductase (non-electrogenic)
This is an abbreviated version!
For detailed information about NADH:quinone reductase (non-electrogenic), go to the full flat file.
Word Map on EC 1.6.5.9
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1.6.5.9
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ndh-2
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hydrogenases
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proton-translocating
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ubiquinone-1
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hqno
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2-heptyl-4-hydroxyquinoline-n-oxide
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single-subunit
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deamino-nadh
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na+-translocating
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rotenone-sensitive
- 1.6.5.9
- ndh-2
- hydrogenases
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proton-translocating
- ubiquinone-1
- hqno
- 2-heptyl-4-hydroxyquinoline-n-oxide
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single-subunit
- deamino-nadh
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na+-translocating
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rotenone-sensitive
Reaction
Synonyms
alternative external NADH dehydrogenase, alternative NADH dehydrogenase, alternative NADH-quinone oxidoreductase, alternative NADH:quinone reductase, alternative NADH:ubiquinone oxidoreductase, alternative rotenone-insensitive NADH:Q oxidoreductase, CathTA2_0279, Cgl1465, EC 1.6.5.11, EC 1.6.99.5, external alternative NADH dehydrogenase, external alternative NADH: ubiquinone oxidoreductase, external NADH:ubiquinone oxidoreductase, external rotenone-insensitive NADH dehydrogenase, internal alternative NADH dehydrogenase, internal alternative NADH: ubiquinone oxidoreductase, internal alternative NADH:ubiquinone oxidoreductase, Internal NADH dehydrogenase, internal rotenone-insensitive NADH dehydrogenase, NADH dehydrogenase, NADH dehydrogenase-2, NADH-ubiquinone oxidoreductase, NADH: ubiquinone oxidoreductase, NADH: ubiquinone-2 oxidoreductase, NADH:Q6 oxidoreductase, NADH:ubiquinone reductase (non-electrogenic), NADHQ2, NDA, NDB, NdeA, NdeA-B, NDH, NDH-2, NDH-II, NDH2, NDH2e, NDH2i, Ndi1, NdiA, NDX, non-proton pumping type II NADH dehydrogenase, non-proton-pumping NADH dehydrogenase, rotenone-insensitive NADH dehydrogenase, rotenone-insensitive NADH-ubiquinone oxidoreductase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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three NADH dehydrogenases, two external rotenone-insensitive NADH:ubiquinone oxidoreductases (NDE1 and NDE2), and one internal rotenone-insensitive NADH:ubiquinone reductase (NDI1)
malfunction
metabolism
NDH2e-derived electrons are channelled to the cytochrome pathway
physiological function
additional information
malfunction
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strains carrying the deletion of NDH2 are completely viable
malfunction
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the induced RNAi cell line exhibits slower growth, decreased mitochondrial membrane potential and lower sensitivity of respiration to inhibitors. Mitochondrial membrane potential is altered in NDH2 knockdown. Growth phenotype of procyclic Trypanosoma brucei interfered against NDH2, overview
malfunction
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the induced RNAi cell line exhibits slower growth, decreased mitochondrial membrane potential and lower sensitivity of respiration to inhibitors. Mitochondrial membrane potential is altered in NDH2 knockdown. Growth phenotype of procyclic Trypanosoma brucei interfered against NDH2, overview
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malfunction
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strains carrying the deletion of NDH2 are completely viable
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physiological function
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internal alternative NADH:ubiquinone oxidoreductase is the only enzyme capable of feeding NADH generated in the mitochondrial matrix into the respiratory chain
physiological function
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isoform NDH2i allows survival of double mutants lacking both complex I and isoform NDH2e
physiological function
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NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
physiological function
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external rotenone-insensitive NADH:ubiquinone oxidoreductases (NDE1 and NDE2), and one internal rotenone-insensitive NADH:ubiquinone reductase (NDI1) are involved in farnesol resistance
physiological function
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NDH2 is a part of the respiratory chain that does not pump protons across the inner membrane. NDH2 is the major NADH: ubiquinone oxidoreductase responsible for cytosolic and not for mitochondrial NAD+ regeneration in the mitochondrion of procyclic Trypanosoma brucei. thatNDH2is facing intermembrane space, rendering complex I responsible only for the regeneration of matrix NAD+. Ability of NDH2 to fully compensate for the loss of complex I. NDH2 is essential for the maintenance of mitochondrial membrane potential in procyclic Trypanosoma brucei
physiological function
inner mitochondrial isoform Ndi1 associates with complexes III and IV. Ndi1 is found in high molecular weight supercomplexes. Complexes containing the NADH dehydrogenase activity are also found in mutants lacking the external NADH dehydrogenases NDE1 and NDE2
physiological function
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Drosophila melanogaster expressing alternative NADH dehydrogenase NDX have 17-71% lifespan prolongation on media with different protein-to-carbohydrate ratios except NDX-expressing males that have 19% shorter lifespan than controls on a high protein diet. NDX-expressing flies are more resistant to 2,4-dichlorophenoxyacetic acid and alloxan, and to potassium iodate, and partially to sodium molybdate treatments. NDX-expressing flies are more sensitive to catechol and sodium chromate
physiological function
in glucose minimal medium the Ndh deletion mutant, but not the strains lacking L-lactate dehydrogenase LdhA and malate dehydrogenase Mdh, shows reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants lacking Ndh/Mdh or Ndh/LdhA, in glucose medium is stronger impaired than that of the Ndh mutant. In L-lactate minimal medium, the Ndh mutant grows better than the wild-type. The Ndh/Mdh double mutant fails to grow in L-lactate medium and acetate medium. Attempts to construct a Ndh/Mdh/LdhA triple mutant failed
physiological function
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in glucose minimal medium the Ndh deletion mutant, but not the strains lacking L-lactate dehydrogenase LdhA and malate dehydrogenase Mdh, shows reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants lacking Ndh/Mdh or Ndh/LdhA, in glucose medium is stronger impaired than that of the Ndh mutant. In L-lactate minimal medium, the Ndh mutant grows better than the wild-type. The Ndh/Mdh double mutant fails to grow in L-lactate medium and acetate medium. Attempts to construct a Ndh/Mdh/LdhA triple mutant failed
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physiological function
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NDH2 is a part of the respiratory chain that does not pump protons across the inner membrane. NDH2 is the major NADH: ubiquinone oxidoreductase responsible for cytosolic and not for mitochondrial NAD+ regeneration in the mitochondrion of procyclic Trypanosoma brucei. thatNDH2is facing intermembrane space, rendering complex I responsible only for the regeneration of matrix NAD+. Ability of NDH2 to fully compensate for the loss of complex I. NDH2 is essential for the maintenance of mitochondrial membrane potential in procyclic Trypanosoma brucei
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physiological function
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NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
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additional information
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NdeA shows a pyridine nucleotide-disulfide oxidoreductase domain, a small NADH binding domain within a larger FAD binding domain at amino acid positions 226-334, and an EF-hand calcium-binding domain at amino acid positions 433-468
additional information
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NDH-2 structure analysis by circular dichroism and Fourier transform infrared spectroscopy using the recombinanatly expressed enzyme and modelling, overview
additional information
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Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the mitochondrial matrix. It is a peripheral membrane protein forming an intimate dimer, in which packing of the monomeric units within the dimer creates an amphiphilic membrane-anchor domain structure. Structures of the Ndi1–NAD+ and Ndi1–UQ2 complexes show overlapping binding sites for the NAD+ and quinone substrates
additional information
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targeted expression of Ndi1 in fly neurons significantly increases lifespan without compromising fertility or physical activity. Expression of the yeast Ndi1 gene in Drosophila mitochondria leads to an increase in respiratory chain activity, overview
