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Enzyme Nomenclature
Information on EC 1.6.99.3 - NADH dehydrogenase
for references in articles please use BRENDA:EC1.6.99.3
Word Map on EC 1.6.99.3
- 1.6.99.3
- succinate
-
mtdnas
- ubiquinone
- superoxide
- atpase
- flavin
- rotenone
- trna
-
flavoproteins
- malate
- antimycin
-
iron-sulfur
-
submitochondrial
- fmn
- aniline
- ferricyanide
-
nadh:ubiquinone
- aminopyrine
- n-demethylase
- echinococcus
- leber
-
heteroplasmic
- semiquinone
-
subcomplexes
-
nadh-cytochrome
-
drug-metabolizing
-
proton-translocating
-
ethoxycoumarin
- granulosus
- myxothiazol
-
proton-pumping
- cumene
-
haplogroups
-
monophyly
- hexobarbital
-
apocytochrome
-
mtdna-encoded
-
homoplasmic
- echinococcosis
- quinol
-
d-loop
- leigh
- benzphetamine
- ethylmorphine
- encephalomyopathy
-
ubiquinol-cytochrome
-
succinate-cytochrome
- mpp+
-
p-nitroanisole
-
phylogeography
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.6.99.3
-
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RECOMMENDED NAME
GeneOntology No.
NADH dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + acceptor = NAD+ + reduced acceptor
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
-
-
reduction
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-
-
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oxidation
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
NADH:acceptor oxidoreductase
A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 1.6.5.3, NADH dehydrogenase (ubiquinone).
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CAS REGISTRY NUMBER
COMMENTARY
9079-67-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes nuoD, nuoG, nuoM encoding components of the NADH dehydrogenase complex
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
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chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
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chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
additional information
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backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
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backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
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backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
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backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
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-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
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-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
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-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
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-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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specific for NADH
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-
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NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
rate of oxidation is less than 5% of the reaction with NADH
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-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
less than 6% of the activity with NADH
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-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
less than 6% of the activity with NADH
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
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activity with NADPH is about 35% of the activity with NADH
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-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
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less active as NADH
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-
?
additional information
?
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the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
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additional information
?
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the enzyme also shows NADH oxidase activity
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additional information
?
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the enzyme transfers electrons from NADH to external oxidants like ferricyanide through pathways which are linked to metabolic processess in the cell
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additional information
?
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with anaerobic NO2-, the most downregulated genes are those involved postglycolytically and include many tricarboxylic acid cycle genes and those involved in the electron transport chain, especially those encoding the NADH dehydrogenase I complex, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
-
-
-
additional information
?
-
-
the enzyme transfers electrons from NADH to external oxidants like ferricyanide through pathways which are linked to metabolic processess in the cell
-
-
-
additional information
?
-
-
with anaerobic NO2-, the most downregulated genes are those involved postglycolytically and include many tricarboxylic acid cycle genes and those involved in the electron transport chain, especially those encoding the NADH dehydrogenase I complex, overview
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
natural prosthetic group of the enzyme, apoenzyme catalyzed reaction with ferricyanide, FAD is required for reaction with 2,6-dichlorophenol or with cytochrome c, Km: 0.00056 mM
FAD
1:1 binding stoichiometry with protein and an association constant K of 70000 per mol. The FAD-protein interaction is energetically favorable and the addition of FAD is not necessary to induce the enzyme folded state
NADPH
-
less than 6% of the activity with NADH in reaction with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferricyanide
-
competitive substrate inhibition due to its direct binding to the enzyme and forming an inactive binary complex
NAD+
FAD-dependent oxidase activity of NADH dehydrogenase is inhibited by NAD+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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activation of the enzyme in erythrocytes by beta-adrenergic agonists
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
benzyl viologen
-
after induction with 1.5% arabinose in culture medium
0.44
methyl viologen
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after induction with 1.5% arabinose in culture medium
1.035
NADPH
-
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
0.06
ferricyanide
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after induction with 1.5% arabinose in culture medium
0.0692
NADH
-
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
0.1
NADH
-
electron acceptor benzyl viologen, after induction with 1.5% arabinose in culture medium
0.22
NADH
-
electron acceptor methyl viologen, after induction with 1.5% arabinose in culture medium
0.31
NADH
-
electron acceptor ferricyanide, after induction with 1.5% arabinose in culture medium
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
650
NADH
-
electron acceptor methyl viologen, after induction with 1.5% arabinose in culture medium
725
NADH
-
electron acceptor benzyl viologen, after induction with 1.5% arabinose in culture medium
1170
NADH
-
electron acceptor ferricyanide, after induction with 1.5% arabinose in culture medium
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
-
substrate Clostridium acetobutylicum ferredoxin, after induction with 1.5% arabinose in culture medium
392
-
substrate methyl viologen, after induction with 1.5% arabinose in culture medium
582
-
substrate benzyl viologen, after induction with 1.5% arabinose in culture medium
604
-
substrate ferricyanide, after induction with 1.5% arabinose in culture medium
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8
-
activity with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
activity with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
digestion of muscle preparation at 37°C with sake-venom phospholipase
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH. NDH subunits form three types of complexes with different subunit compositions. NDH-1L is required for heterotrophic growth, probably via respiration and CET, while NDH-1M and NDH-1S form the NDH-1MS complex that functions in CO2 concentration
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
0.0004 mg phospholipid per mg of protein, most of which is cardiolipin with traces of phosphatidylethanolamine and phosphatidylglycerol
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, active protein as well as individual subunits are expressed separately
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expression in Escherichia coli
genes nuoD, nuoG, nuoM encoding components of the NADH dehydrogenase complex, construction of a signature-tagged mutagenesis library of Pseudomonas aeruginosa, genes regulated by NO2-, anaerobically induced, transcriptional profiling, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K308A
one third of oxidase activity of the wild type NADH dehydrogenase
G478A
-
no NADH dehydrogenase activity and NADH oxidase activity which appears to result from
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