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Information on EC 1.6.5.9 - NADH:ubiquinone reductase (non-electrogenic) Word Map on EC 1.6.5.9
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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NADH:ubiquinone reductase (non-electrogenic)
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NADH + H+ + ubiquinone = NAD+ + ubiquinol
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NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)
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aerobic respiration II (cytochrome c) (yeast)
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NADH to cytochrome bd oxidase electron transfer II
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NADH to cytochrome bo oxidase electron transfer II
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nitrate reduction VIIIb (dissimilatory)
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NADH:ubiquinone oxidoreductase
A flavoprotein (FAD). Occurs in mitochondria of yeast and plants, and in aerobic bacteria. Has low activity with NADPH.
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alternative external NADH dehydrogenase
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alternative NADH dehydrogenase
alternative NADH-quinone oxidoreductase
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alternative NADH:quinone reductase
alternative NADH:ubiquinone oxidoreductase
alternative rotenone-insensitive NADH:Q oxidoreductase
external alternative NADH dehydrogenase
external alternative NADH: ubiquinone oxidoreductase
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external NADH:ubiquinone oxidoreductase
external rotenone-insensitive NADH dehydrogenase
internal alternative NADH dehydrogenase
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internal alternative NADH: ubiquinone oxidoreductase
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internal alternative NADH:ubiquinone oxidoreductase
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Internal NADH dehydrogenase
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internal rotenone-insensitive NADH dehydrogenase
NADH-ubiquinone oxidoreductase
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NADH: ubiquinone oxidoreductase
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NADH: ubiquinone-2 oxidoreductase
NADH:Q6 oxidoreductase
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non-proton-pumping NADH dehydrogenase
rotenone-insensitive NADH dehydrogenase
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alternative NADH dehydrogenase
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alternative NADH dehydrogenase
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alternative NADH dehydrogenase
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alternative NADH dehydrogenase
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alternative NADH:quinone reductase
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alternative NADH:quinone reductase
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alternative NADH:ubiquinone oxidoreductase
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alternative NADH:ubiquinone oxidoreductase
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alternative NADH:ubiquinone oxidoreductase
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alternative rotenone-insensitive NADH:Q oxidoreductase
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alternative rotenone-insensitive NADH:Q oxidoreductase
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external alternative NADH dehydrogenase
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external alternative NADH dehydrogenase
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external NADH:ubiquinone oxidoreductase
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external NADH:ubiquinone oxidoreductase
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external rotenone-insensitive NADH dehydrogenase
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isoform NDB
external rotenone-insensitive NADH dehydrogenase
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isoform NDB
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internal rotenone-insensitive NADH dehydrogenase
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isoform NDA
internal rotenone-insensitive NADH dehydrogenase
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isoform NDA
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NADH: ubiquinone-2 oxidoreductase
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NADH: ubiquinone-2 oxidoreductase
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NADHQ2
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NDA
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isoform
NDB
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isoform
NDH-II
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NDH2
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NDH2e
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isoform
NDH2i
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internal version of alternative NADH:ubiquinone oxidoreductase
Ndi1
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Ndi1
an NDH-2-type alternative NADH-quinone oxidoreductase
non-proton-pumping NADH dehydrogenase
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non-proton-pumping NADH dehydrogenase
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brenda
genes ndeA-B and ndiA encoding external and internal alternative NADH dehydrogenases
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brenda
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brenda
formerly Gluconobacter suboxydans strain IFO12528
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brenda
formerly Gluconobacter suboxydans strain IFO12528
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
gene Ndi1
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brenda
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brenda
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UniProt
brenda
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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)
metabolism
NDH2e-derived electrons are channelled to the cytochrome pathway
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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isoform NDH2i allows survival of double mutants lacking both complex I and isoform NDH2e
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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NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
physiological function
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NDI1 cannot promote proton pumping
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
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NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
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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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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
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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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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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 Ndi1āNAD+ and Ndi1āUQ2 complexes show overlapping binding sites for the NAD+ and quinone substrates
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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
NADH + H+ + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
NADH + H+ + 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
?
NADH + H+ + 2-azido-5-geranyl-3-methoxy-6-methyl-1,4-benzoquinone
NAD+ + 2-azido-5-geranyl-3-methoxy-6-methyl-1,4-benzoquinol
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-
?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
NADH + H+ + duroquinone
NAD+ + duroquinol
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49% activity compared to ubiquinone-1
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?
NADH + H+ + juglone
NAD+ + ?
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29% activity compared to ubiquinone-1
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?
NADH + H+ + menadione
NAD+ + menadiol
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47% activity compared to ubiquinone-1
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?
NADH + H+ + menaquinone
NAD+ + menaquinol
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?
NADH + H+ + N-(6-[[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]amino]-6-oxohexyl)-6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
NAD+ + N-(6-[[(4E,8E)-10-(4-azido-3,6-dihydroxy-5-methoxy-2-methylcyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]amino]-6-oxohexyl)-6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
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-
?
NADH + H+ + n-decylubiquinone
NAD+ + n-decylubiquinol
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?
NADH + H+ + N-[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]-6-([5-[(3aS,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
NAD+ + N-[(4E,8E)-10-(4-azido-3,6-dihydroxy-5-methoxy-2-methylcyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]-6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
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-
?
NADH + H+ + N-[2-[2-(2-[[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]oxy]ethoxy)ethoxy]ethyl]-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide
NAD+ + N-[2-[2-(2-[[(4E,8E)-10-(4-azido-3,6-dihydroxy-5-methoxy-2-methylcyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]oxy]ethoxy)ethoxy]ethyl]-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide
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-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
NADH + H+ + ubiquinone-10
NAD+ + ubiquinol-10
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?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
NADH + H+ + ubiquinone-6
NAD+ + ubiquinol-6
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-
?
additional information
?
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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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15% activity compared to ubiquinone-1
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?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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-
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?
NADH + H+ + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
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17% activity compared to ubiquinone-1
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?
NADH + H+ + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
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?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
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?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
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100% activity
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-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
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-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
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-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
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-
-
?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
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?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
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ubiquinone is the best electron acceptor
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?
additional information
?
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no activity with cytochrome c
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additional information
?
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NDH-II does not pump protons
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additional information
?
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NDH-II does not pump protons
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additional information
?
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the yeast enzyme is a two-electron reaction enzyme
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additional information
?
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NAD+ binds in the second Rossmann domain in a predominantly positively charged cleft, with the nicotinamide ring approaching the re-face of the FAD
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additional information
?
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the alternative NADH:ubiquinone oxidoreductase does not contribute to the proton gradient across the respiratory membrane
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additional information
?
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alternative NADH:ubiquinone oxidoreductase does not pump protons across the inner mitochondrial membrane
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additional information
?
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NDH2 does not translocate protons across the inner mitochondrial membrane
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additional information
?
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NDH2e is a peripheral single-subunit oxido-reductase that does not pump protons
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additional information
?
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alternative NADH:ubiquinone oxidoreductase does not pump protons across the inner mitochondrial membrane
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NADH + H+ + ubiquinone
NAD+ + ubiquinol
additional information
?
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the alternative NADH:ubiquinone oxidoreductase does not contribute to the proton gradient across the respiratory membrane
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NADH + H+ + ubiquinone
NAD+ + ubiquinol
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
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?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
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-
?
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NADPH
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below pH 7.0 NADPH is slowly oxidized
FAD
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non-covalently linked
FAD
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the mature enzyme contains FAD as prosthetic group
FAD
Ndi1 contains noncovalently bound FAD
FAD
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the enzyme contains one molecule of noncovalently bound FAD as redox cofactor
FAD
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binding site structure, overview. The isoalloxazine ring of the FAD is positioned between the two Rossmann domains, which define two channels along the interdomain plane that lead to the active site
NADH
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the enzyme is specific for NADH. NADPH or deamino-NADH show rates that are at least 250times lower than obtained with NADH at any pH between 5.5 and 8.5
NADH
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the partially purified enzyme is specific for NADH above pH 7.0
NADH
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small NADH binding domain within a larger FAD binding domain at amino acid positions 226-334
NADH
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binding site structure, overview
additional information
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the enzyme contains no iron-sulfur clusters
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additional information
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the mature enzyme contains no iron-sulfur clusters
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additional information
Ndi1 contains no iron-sulfur cluster
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additional information
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the enzyme lacks iron-sulfur clusters
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additional information
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no iron-sulfur centers
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1-hydroxy-2-dodecyl-4(1H)quinolone
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28% residual activity at 0.01 mM
2,6-dichlorophenolindophenol
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substrate inhibition
aculeacin A
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63% residual activity at 0.005 mg/ml
AMP
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dead end reversible inhibitor, competitive inhibitor of NADH and uncompetitive inhibitor of 2,6-dichlorophenolindophenol
aurachin analogue AC0-10
specific inhibitor
aurachin C 1-10
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12% residual activity at 0.01 mM, noncompetitive inhibitor
funiculosin
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68% residual activity at 0.005 mg/ml
Gramicidin S
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31% residual activity at 0.005 mg/ml
NADH
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substrate inhibition
polymixin B
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51% residual activity at 0.005 mg/ml
reduced 2,6-dichlorophenolindophenol
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product inhibition
rotenone
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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)
scopafungin
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33% residual activity at 0.005 mg/ml, noncompetitive inhibitor
staurosporine
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70% residual activity at 0.005 mg/ml
flavone
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flavone
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partial inhibitor
additional information
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the enzyme is not inhibited by rotenone, and activity is not affected by EDTA (1 mM), EGTA (1 mM) or Ca2+ or Mg2+ (1 mM)
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additional information
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NADH oxidation is completely insensitive to amytal and rotenone
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additional information
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NAD+, Mg-ADP, Mg-ATP, Ca2+ (all at 2 mM) or piericidin, rotenone (both at 0.01 mM) or adenosyl-3'-O-[3-[N-(4-azido-2-nitrophenyl)-amino]propionyl]-NAD+ (0.05 mM) are without inhibitory or stimulatory effects
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additional information
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not inhibited by rotenone, NAD+ does not inhibit the activity of the enzyme, even at concentrations as high as 10 mM
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additional information
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Ndi1 is rotenone-insensitive
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additional information
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the enzyme is rotenone-insensitive
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additional information
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the enzyme is rotenone-insensitive
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additional information
insensitive to rotenone
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additional information
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not inhibited by piericidin A. Addition of up to 10% (v/v) ethanol has no effect on NADH:NBQ oxidoreductase activity
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0.0062
2,6-dichlorophenolindophenol
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pH 7.0, 25°C
0.0181
N-(6-[[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]amino]-6-oxohexyl)-6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication
0.022
N-[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]-6-([5-[(3aS,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanamide
in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication
0.033
N-[2-[2-(2-[[(4E,8E)-10-(4-azido-5-methoxy-2-methyl-3,6-dioxocyclohexa-1,4-dien-1-yl)-4,8-dimethyldeca-4,8-dien-1-yl]oxy]ethoxy)ethoxy]ethyl]-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide
in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication
0.0152
ubiquinone-1
in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication
0.0079
ubiquinone-2
in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication
0.0094
NADH
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pH 7.0, 25°C
0.014
NADH
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pH and temperature not specified in the publication
0.028
NADH
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at 25°C and pH 7.2
0.157
NADH
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at 25°C in 100mM Tris-HCl (pH 7.4)
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0.031
NADH
-
using ubiquinone-2 as substrate, in 20 mM MOPS/KOH, 1 mM EDTA, 0.03% (v/v) Triton X-100, 200 mM KCl, pH 6.2, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1152
2,6-dichlorophenolindophenol
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pH 7.0, 25°C
0.0014
Gramicidin S
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at 25°C in 100mM Tris-HCl (pH 7.4)
0.0525
NADH
-
pH 7.0, 25°C
0.0141
reduced 2,6-dichlorophenolindophenol
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pH 7.0, 25°C
0.0055
scopafungin
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at 25°C in 100mM Tris-HCl (pH 7.4)
5.5
AMP
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linear competitive inhibition of NADH, pH 7.0, 25°C
11.5
AMP
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linear uncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C
0.0054
flavone
-
hyperbolic uncompetitive inhibition of NADH, pH 7.0, 25°C
0.0071
flavone
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hyperbolic noncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0017
1-hydroxy-2-dodecyl-4(1H)quinolone
Gluconobacter oxydans
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at 25°C in 100mM Tris-HCl (pH 7.4)
0.00034
aurachin C 1-10
Gluconobacter oxydans
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at 25°C in 100mM Tris-HCl (pH 7.4)
0.0012
Gramicidin S
Gluconobacter oxydans
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at 25°C in 100mM Tris-HCl (pH 7.4)
0.0062
scopafungin
Gluconobacter oxydans
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at 25°C in 100mM Tris-HCl (pH 7.4)
0.095
flavone
Saccharomyces cerevisiae
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using ubiquinone-2 as substrate, in 20 mM MOPS/KOH, 1 mM EDTA, 0.03% (v/v) Triton X-100, 200 mM KCl, pH 6.2, temperature not specified in the publication
0.175
flavone
Arum maculatum
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at 25°C and pH 7.2
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0.78
-
crude extract, using ubiquinone-2 as substrate, at pH 6.2, temperature not specified in the publication
3.7
-
crude enzyme, using ubiquinone-1 as substrate, at 25°C and pH 7.2
61.9
-
after 2134fold purification, using ubiquinone-6 as substrate, at pH 6.2, temperature not specified in the publication
69.2
-
after 18.7fold purification, using ubiquinone-1 as substrate, at 25°C and pH 7.2
1671
-
after 2134fold purification, using ubiquinone-2 as substrate, at pH 6.2, temperature not specified in the publication
3372
-
crude enzyme, using ubiquinone-1 as substrate, at 25°C and pH 7.2
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6.2
-
with ubiquinone-2 as acceptor a sharp maximum at pH 6.2 is obtained
7.2
-
pH-optimum around pH 7.2
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4.5 - 9.5
-
with ubiquinone-6 as acceptor the activity is almost constant between pH 4.5 and 9.5, at pH values lower than 4.5 and higher than 9.5, enzymic activity is irreversibly destroyed
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8.5
native enzyme, calculated from amino acid sequence
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-
-
brenda
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NDH-II is bound peripherally to the inner surface of the cytoplasmic membrane
-
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NDH-II is bound peripherally to the inner surface of the cytoplasmic membrane
-
-
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the enzyme is peripheral membrane-bound
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Ndi1 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, membrane-anchor domain, overview
brenda
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-
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mitochondrial inner membrane
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outer surface of the inner mitochondrial membrane
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NDH2 is oriented towards the external face of the mitochondrial inner membrane
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NDH2 is oriented towards the external face of the mitochondrial inner membrane
-
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Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix
brenda
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after import, isoform NDA is intramitochondrially sorted to the matrix side of the inner membrane, whereas isoform NDB becomes exposed to the intermembrane space
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after import, isoform NDA is intramitochondrially sorted to the matrix side of the inner membrane, whereas isoform NDB becomes exposed to the intermembrane space
-
brenda
-
alternative NADH dehydrogenase activity is located exclusively at the external face of the mitochondrial inner membrane
brenda
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Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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33900
-
the rotenone-insensitive NADH-ubiquinone-1 reductase activity eluted by 0.5 M NaCl displays three major bands on SDS-PAGE of 55000, 39200 and 33900 Da
39200
-
the rotenone-insensitive NADH-ubiquinone-1 reductase activity eluted by 0.5 M NaCl displays three major bands on SDS-PAGE of 55000, 39200 and 33900 Da
52000
-
isoform NDA, SDS-PAGE
65000
-
isoform NDB, calculated from amino acid sequence
65800
-
calculated from amino acid sequence
53000
-
SDS-PAGE
53000
estimated from amino acid sequence
55000
-
isoform NDH2i, SDS-PAGE
55000
-
the rotenone-insensitive NADH-ubiquinone-1 reductase activity eluted by 0.5 M NaCl displays three major bands on SDS-PAGE of 55000, 39200 and 33900 Da
55000
-
isoform NDA, calculated from amino acid sequence
60000
-
isoform NDH2e, SDS-PAGE
60000
-
isoform NDB, SDS-PAGE
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additional information
-
NDH-2 structure analysis by circular dichroism and Fourier transform infrared spectroscopy using the recombinanatly expressed enzyme and modelling, overview
monomer
-
1 * 53000, SDS-PAGE
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Ndi1 in its substrate-free, NAD+- and ubiquinone-complexed states, X-ray diffraction structure determination and analysis
-
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5.5 - 8
-
the free enzyme and the binary complex E-NADH are highly stable in the pH range from 5.5 to 8.0, maintaining the initial activity after 10 min incubation. Maximal stability is observed at pH 5.0 and 6.5 with no loss in activity. The enzyme is highly unstable above and below this pH range
392700
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the enzyme is stable at low protein concentrations and in the presence of both substrates
-
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5'-ADP-Sepharose 4B column chromatography
-
DEAE Bio-gel column chromatography and Blue Sepharose CL-6B column chromatography, column chromatography
-
DEAE-cellulose column chromatography and blue Sepharose CL-6B column chromatography
-
DEAE-Sepharose column chromatography
recombinant His-tagged NDH-2 by nickel affinity chromatography
-
streptavidin-agarose chromatography
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expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli membranes
gene Ndi1, inducible NDI1 enzyme expression in Drosophila melanogaster mitochondria of different cells and tissues. Expression of Ndi1 in fly mitochondria leads to an increase in NADH-ubiquinone oxidoreductase activity, oxygen consumption and ATP levels. In addition, exogenous Ndi1 expression results in increased CO2 production in living flies. Targeted expression of Ndi1 in fly neurons significantly increases lifespan without compromising fertility or physical activity
-
recombinant expression of His-tagged NDH-2
-
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the amount of enzyme in the cell is subject to glucose repression, it increases slightly when cells, grown on glucose or lactate, enter the stationary phase
-
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additional information
-
when exposed to farnesol, the DELTAaifA and DELTAndeA strains have increased reactive oxygen species production while DndeB, DELTAndeA DELTAndeB, and DELTAndiA mutant strains show the same reactive oxygen species accumulation than in the absence of farnesol
additional information
-
NDH2 gene silencing using tetracycline-inducible RNAi
additional information
-
NDH2 gene silencing using tetracycline-inducible RNAi
-
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NDA1_ARATH
510
56628
Swiss-Prot
NDA1_SOLTU
495
54902
Swiss-Prot
NDA2_ARATH
508
56503
Swiss-Prot
NDB1_ARATH
571
63314
Swiss-Prot
NDB3_ARATH
580
65164
Swiss-Prot
NDB1_SOLTU
577
65155
Swiss-Prot
NDB2_ARATH
582
65059
Swiss-Prot
NDB4_ARATH
582
65372
Swiss-Prot
INDA1_SOLTU
495
54911
Swiss-Prot
NDC1_ARATH
519
56916
Swiss-Prot
NDI1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
513
57250
Swiss-Prot
ENDB1_SOLTU
577
65189
Swiss-Prot
NDH1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
551
61675
Swiss-Prot
NDH1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
560
62774
Swiss-Prot
NDH2_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
551
60781
Swiss-Prot
NDH2_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
582
65815
Swiss-Prot
NDH2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
545
61659
Swiss-Prot
A0A1D7ZUM0_LACFE
414
44704
TrEMBL
W0BI37_9GAMM
288
31896
TrEMBL
A0A1G4G9E6_9PORP
412
46648
TrEMBL
I7J5C6_BABMR
Babesia microti (strain RI)
554
62579
TrEMBL
A0A0F8AWR2_CERFI
583
64204
TrEMBL
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De Vries, S.; Grivell, L.A.
Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
Eur. J. Biochem.
176
377-384
1988
Saccharomyces cerevisiae
brenda
Velazquez, I.; Pardo, J.P.
Kinetic characterization of the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
389
7-14
2001
Saccharomyces cerevisiae
brenda
Garofano, A.; Eschemann, A.; Brandt, U.; Kerscher, S.
Substrate-inducible versions of internal alternative NADH: ubiquinone oxidoreductase from Yarrowia lipolytica
Yeast
23
1129-1136
2006
Yarrowia lipolytica
brenda
Murai, M.; Yamashita, T.; Senoh, M.; Mashimo, Y.; Kataoka, M.; Kosaka, H.; Matsuno-Yagi, A.; Yagi, T.; Miyoshi, H.
Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling
Biochemistry
49
2973-2980
2010
Saccharomyces cerevisiae (P32340), Saccharomyces cerevisiae
brenda
Kerscher, S.
Diversity and origin of alternative NADH:ubiquinone oxidoreductases
Biochim. Biophys. Acta
1459
274-283
2000
Saccharomyces carlsbergensis
brenda
Guerrero-Castillo, S.; Vazquez-Acevedo, M.; Gonzalez-Halphen, D.; Uribe-Carvajal, S.
In Yarrowia lipolytica mitochondria, the alternative NADH dehydrogenase interacts specifically with the cytochrome complexes of the classic respiratory pathway
Biochim. Biophys. Acta
1787
75-85
2009
Yarrowia lipolytica (F2Z699), Yarrowia lipolytica
brenda
Cook, N.; Cammack, R.
Purification and characterization of the rotenone-insensitive NADH dehydrogenase of mitochondria from Arum maculatum
Eur. J. Biochem.
141
573-577
1984
Arum maculatum
brenda
Mogi, T.; Matsushita, K.; Murase, Y.; Kawahara, K.; Miyoshi, H.; Ui, H.; Shiomi, K.; Omura, S.; Kita, K.
Identification of new inhibitors for alternative NADH dehydrogenase (NDH-II): Research Letter
FEMS Microbiol. Lett.
291
157-161
2009
Gluconobacter oxydans, Gluconobacter oxydans NBRC3172
brenda
Kerscher, S.; Okun, J.; Brandt, U.
A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
J. Cell Sci.
112
2347-2354
1999
Yarrowia lipolytica, Yarrowia lipolytica E150
brenda
Kerscher, S.; Eschemann, A.; Okun, P.; Brandt, U.
External alternative NADH: ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica
J. Cell Sci.
114
3915-3921
2001
Yarrowia lipolytica
brenda
Rasmusson, A.; Svensson, A.; Knoop, V.; Grohmann, L.; Brennicke, A.
Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: Two enzymes are present in potato mitochondria
Plant J.
20
79-87
1999
Solanum tuberosum, Solanum tuberosum cultivar Desiree
brenda
Bahadorani, S.; Cho, J.; Lo, T.; Contreras, H.; Lawal, H.O.; Krantz, D.E.; Bradley, T.J.; Walker, D.W.
Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreductase (Ndi1) extends Drosophila lifespan
Aging Cell
9
191-202
2010
Saccharomyces cerevisiae
brenda
Villegas, J.M.; Torres-Bugeau, C.M.; Chehin, R.; Burgos, M.I.; Fidelio, G.D.; Rintoul, M.R.; Rapisarda, V.A.
Maintenance and thermal stabilization of NADH dehydrogenase-2 conformation upon elimination of its C-terminal region
Biochimie
95
382-387
2013
Escherichia coli
brenda
Dinamarco, T.; Figueiredo Pimentel, B.; Savoldi, M.; Malavazi, I.; Soriani, F.; Uyemura, S.; Ludovico, P.; Goldman, M.; Goldman, G.
The roles played by Aspergillus nidulans apoptosis-inducing factor (AIF)-like mitochondrial oxidoreductase (AifA) and NADH-ubiquinone oxidoreductases (NdeA-B and NdiA) in farnesol resistance
Fungal Genet. Biol.
47
1055-1069
2010
Aspergillus nidulans
brenda
Verner, Z.; Skodova, I.; Polakova, S.; Durisova-Benkovicova, V.; Horvath, A.; Lukes, J.
Alternative NADH dehydrogenase (NDH2): intermembrane-space-facing counterpart of mitochondrial complex I in the procyclic Trypanosoma brucei
Parasitology
140
328-337
2013
Trypanosoma brucei, Trypanosoma brucei 29-13
brenda
Iwata, M.; Lee, Y.; Yamashita, T.; Yagi, T.; Iwata, S.; Cameron, A.D.; Maher, M.J.
The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates
Proc. Natl. Acad. Sci. USA
109
15247-15252
2012
Saccharomyces cerevisiae
brenda
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