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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
EC 1.6.5.11
-
-
formerly
-
EC 1.6.99.5
-
-
formerly
-
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-ubiquinone oxidoreductase
-
-
NADH: ubiquinone oxidoreductase
-
-
NADH: ubiquinone-2 oxidoreductase
NADH:Q6 oxidoreductase
-
-
NADH:ubiquinone reductase (non-electrogenic)
-
-
-
-
non-proton pumping type II NADH dehydrogenase
non-proton-pumping NADH dehydrogenase
rotenone-insensitive NADH dehydrogenase
-
-
rotenone-insensitive NADH-ubiquinone oxidoreductase
-
alternative NADH dehydrogenase
-
-
alternative NADH dehydrogenase
-
-
alternative NADH dehydrogenase
-
-
-
alternative NADH dehydrogenase
-
-
alternative NADH:quinone reductase
-
-
alternative NADH:quinone reductase
-
-
-
alternative NADH:ubiquinone oxidoreductase
-
-
alternative NADH:ubiquinone oxidoreductase
-
-
alternative NADH:ubiquinone oxidoreductase
-
-
-
alternative rotenone-insensitive NADH:Q oxidoreductase
-
-
alternative rotenone-insensitive NADH:Q oxidoreductase
-
-
-
CathTA2_0279
-
Cgl1465
-
external alternative NADH dehydrogenase
-
-
external alternative NADH dehydrogenase
-
-
external NADH:ubiquinone oxidoreductase
-
-
external NADH:ubiquinone oxidoreductase
-
-
-
external rotenone-insensitive NADH dehydrogenase
-
isoform NDB
external rotenone-insensitive NADH dehydrogenase
-
isoform NDB
-
internal rotenone-insensitive NADH dehydrogenase
-
isoform NDA
internal rotenone-insensitive NADH dehydrogenase
-
isoform NDA
-
NADH: ubiquinone-2 oxidoreductase
-
-
NADH: ubiquinone-2 oxidoreductase
-
-
-
NADHQ2
-
-
NDA
-
isoform
NDB
-
isoform
NDH
-
NDH-II
-
-
NDH2
-
-
NDH2e
-
isoform
NDH2i
-
internal version of alternative NADH:ubiquinone oxidoreductase
Ndi1
-
-
Ndi1
an NDH-2-type alternative NADH-quinone oxidoreductase
non-proton pumping type II NADH dehydrogenase
-
non-proton pumping type II NADH dehydrogenase
-
-
non-proton-pumping NADH dehydrogenase
-
-
non-proton-pumping NADH dehydrogenase
-
-
-
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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
-
-
-
-
?
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
-
-
-
?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
NADH + H+ + duroquinone
NAD+ + duroquinol
-
49% activity compared to ubiquinone-1
-
-
?
NADH + H+ + juglone
NAD+ + ?
-
29% activity compared to ubiquinone-1
-
-
?
NADH + H+ + menadione
NAD+ + menadiol
NADH + H+ + menaquinone
NAD+ + menaquinol
-
-
-
-
?
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
-
-
-
?
NADH + H+ + n-decylubiquinone
NAD+ + n-decylubiquinol
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
NADH + H+ + ubiquinone-10
NAD+ + ubiquinol-10
-
-
-
-
?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
NADH + H+ + ubiquinone-6
NAD+ + ubiquinol-6
-
-
-
-
?
additional information
?
-
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
15% activity compared to ubiquinone-1
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
NADH + H+ + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
-
17% activity compared to ubiquinone-1
-
-
?
NADH + H+ + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
-
-
-
-
?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
-
-
-
-
?
NADH + H+ + 5-nonylubiquinone
NAD+ + 5-nonylubiquinol
-
-
-
-
?
NADH + H+ + menadione
NAD+ + menadiol
-
47% activity compared to ubiquinone-1
-
-
?
NADH + H+ + menadione
NAD+ + menadiol
-
-
-
?
NADH + H+ + menadione
NAD+ + menadiol
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
100% activity
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
-
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
-
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
-
-
?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
-
-
-
?
NADH + H+ + ubiquinone-2
NAD+ + ubiquinol-2
-
ubiquinone is the best electron acceptor
-
-
?
additional information
?
-
-
no activity with cytochrome c
-
-
?
additional information
?
-
-
NDH-II does not pump protons
-
-
?
additional information
?
-
-
NDH-II does not pump protons
-
-
?
additional information
?
-
-
the yeast enzyme is a two-electron reaction enzyme
-
-
?
additional information
?
-
-
NAD+ binds in the second Rossmann domain in a predominantly positively charged cleft, with the nicotinamide ring approaching the re-face of the FAD
-
-
?
additional information
?
-
-
the alternative NADH:ubiquinone oxidoreductase does not contribute to the proton gradient across the respiratory membrane
-
-
?
additional information
?
-
-
alternative NADH:ubiquinone oxidoreductase does not pump protons across the inner mitochondrial membrane
-
-
?
additional information
?
-
-
NDH2 does not translocate protons across the inner mitochondrial membrane
-
-
?
additional information
?
-
NDH2e is a peripheral single-subunit oxido-reductase that does not pump protons
-
-
?
additional information
?
-
-
NDH2e is a peripheral single-subunit oxido-reductase that does not pump protons
-
-
?
additional information
?
-
-
alternative NADH:ubiquinone oxidoreductase does not pump protons across the inner mitochondrial membrane
-
-
?
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1-hydroxy-2-dodecyl-4(1H)quinolone
-
28% residual activity at 0.01 mM
2,6-dichlorophenolindophenol
-
substrate inhibition
aculeacin A
-
63% residual activity at 0.005 mg/ml
AMP
-
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
-
12% residual activity at 0.01 mM, noncompetitive inhibitor
funiculosin
-
68% residual activity at 0.005 mg/ml
Gramicidin S
-
31% residual activity at 0.005 mg/ml
mangostin
20 microM, 19% residual activity for detergent-solubilized enzyme
morin
20 microM, 32% residual activity for detergent-solubilized enzyme, 18.7% residual activity for lipid-reconstituted enzyme
NADH
-
substrate inhibition
nordihydroguaiaretic acid
20 microM, 33% residual activity for detergent-solubilized enzyme, 18.7% residual activity for lipid-reconstituted enzyme
piceatannol
20 microM, 35% residual activity for detergent-solubilized enzyme
polymixin B
-
51% residual activity at 0.005 mg/ml
reduced 2,6-dichlorophenolindophenol
-
product inhibition
rotenone
-
three NADH dehydrogenases, two external rotenone-insensitive NADH:ubiquinone oxidoreductases (NDE1 and NDE2), and one internal rotenone-insensitive NADH:ubiquinone reductase (NDI1)
scopafungin
-
33% residual activity at 0.005 mg/ml, noncompetitive inhibitor
staurosporine
-
70% residual activity at 0.005 mg/ml
tyrphostin AG 537
20 microM, 22% residual activity for detergent-solubilized enzyme, 57% residual activity for lipid-reconstituted enzyme
tyrphostin AG 808
20 microM, 7% residual activity for detergent-solubilized enzyme
flavone
-
-
flavone
-
partial inhibitor
additional information
-
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)
-
additional information
-
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
-
additional information
-
not inhibited by rotenone, NAD+ does not inhibit the activity of the enzyme, even at concentrations as high as 10 mM
-
additional information
-
Ndi1 is rotenone-insensitive
-
additional information
-
NADH oxidation is completely insensitive to amytal and rotenone
-
additional information
-
the enzyme is rotenone-insensitive
-
additional information
-
the enzyme is rotenone-insensitive
-
additional information
insensitive to rotenone
-
additional information
-
insensitive to rotenone
-
additional information
-
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
-
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
-
pH 7.0, 25°C
0.014
NADH
-
pH and temperature not specified in the publication
0.028
NADH
-
at 25°C and pH 7.2
0.157
NADH
-
at 25°C in 100mM Tris-HCl (pH 7.4)
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evolution
-
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
-
strains carrying the deletion of NDH2 are completely viable
malfunction
-
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
-
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
-
strains carrying the deletion of NDH2 are completely viable
-
physiological function
-
internal alternative NADH:ubiquinone oxidoreductase is the only enzyme capable of feeding NADH generated in the mitochondrial matrix into the respiratory chain
physiological function
-
isoform NDH2i allows survival of double mutants lacking both complex I and isoform NDH2e
physiological function
-
NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
physiological function
-
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
-
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
-
NDI1 cannot promote proton pumping
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
-
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
-
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
-
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
-
NDH-II is a key enzyme for the regeneration of an oxidized form of NAD
-
additional information
-
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
-
NDH-2 structure analysis by circular dichroism and Fourier transform infrared spectroscopy using the recombinanatly expressed enzyme and modelling, overview
additional information
-
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 Ndi1NAD+ and Ndi1UQ2 complexes show overlapping binding sites for the NAD+ and quinone substrates
additional information
-
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
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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 pastorianus
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
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