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Information on EC 7.1.1.2 - NADH:ubiquinone reductase (H+-translocating) and Organism(s) Plasmodium falciparum and UniProt Accession Q8I302
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7.1.1.2 NADH:ubiquinone reductase (H+-translocating)IUBMB Comments
The enzyme is a very large complex that participates in electron transfer chains of mitochondria and aerobic bacteria, transferring electrons from NADH to the ubiquinone pool. Reversed electron transport through this enzyme can reduce NAD+ to NADH.
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
complex i, complex 1, nadh dehydrogenase, mitochondrial complex i, grim-19, respiratory complex i, respiratory chain complex i, nadh:ubiquinone oxidoreductase, mitochondrial nadh dehydrogenase, ndh-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
13 kDa differentiation-associated protein
-
-
-
-
CDA016
-
-
-
-
Cell adhesion protein SQM1
-
-
-
-
Cell death-regulatory protein GRIM-19
-
-
-
-
CGI-39
-
-
-
-
CI-11KD
-
-
-
-
CI-12KD
-
-
-
-
CI-14.8KD
-
-
-
-
CI-14KD
-
-
-
-
CI-15 kDa
-
-
-
-
CI-16KD
-
-
-
-
CI-17.3KD
-
-
-
-
CI-17.8KD
-
-
-
-
CI-18 kDa
-
-
-
-
CI-18Kd
-
-
-
-
CI-19.3KD
-
-
-
-
CI-19KD
-
-
-
-
CI-20KD
-
-
-
-
CI-21KD
-
-
-
-
CI-22.5Kd
-
-
-
-
CI-23KD
-
-
-
-
CI-27KD
-
-
-
-
CI-28.5KD
-
-
-
-
CI-29.9KD
-
-
-
-
CI-29KD
-
-
-
-
CI-30KD
-
-
-
-
CI-31KD
-
-
-
-
CI-38.5KD
-
-
-
-
CI-39KD
-
-
-
-
CI-40KD
-
-
-
-
CI-42.5KD
-
-
-
-
CI-42KD
-
-
-
-
CI-49KD
-
-
-
-
CI-51KD
-
-
-
-
CI-75KD
-
-
-
-
CI-78KD
-
-
-
-
CI-9.5
-
-
-
-
CI-9KD
-
-
-
-
CI-AGGG
-
-
-
-
CI-AQDQ
-
-
-
-
CI-ASHI
-
-
-
-
CI-B12
-
-
-
-
CI-B14
-
-
-
-
CI-B14.5a
-
-
-
-
CI-B14.5b
-
-
-
-
CI-B15
-
-
-
-
CI-B16.6
-
-
-
-
CI-B17
-
-
-
-
CI-B17.2
-
-
-
-
CI-B18
-
-
-
-
CI-B22
-
-
-
-
CI-B8
-
-
-
-
CI-B9
-
-
-
-
CI-KFYI
-
-
-
-
CI-MLRQ
-
-
-
-
CI-MNLL
-
-
-
-
CI-MWFE
-
-
-
-
CI-PDSW
-
-
-
-
CI-PGIV
-
-
-
-
CI-SGDH
-
-
-
-
CIB17.2
-
-
-
-
coenzyme Q reductase
-
-
-
-
complex I (electron transport chain)
-
-
-
-
complex I (mitochondrial electron transport)
-
-
-
-
complex I (NADH:Q1 oxidoreductase)
-
-
-
-
complex I dehydrogenase
-
-
-
-
Complex I-11KD
-
-
-
-
Complex I-12KD
-
-
-
-
Complex I-14.8KD
-
-
-
-
Complex I-14KD
-
-
-
-
Complex I-15 kDa
-
-
-
-
Complex I-16KD
-
-
-
-
Complex I-17.3KD
-
-
-
-
Complex I-17.8KD
-
-
-
-
Complex I-18 kDa
-
-
-
-
Complex I-18Kd
-
-
-
-
Complex I-19.3KD
-
-
-
-
Complex I-19KD
-
-
-
-
Complex I-20KD
-
-
-
-
Complex I-21KD
-
-
-
-
Complex I-22.5Kd
-
-
-
-
Complex I-23KD
-
-
-
-
Complex I-27KD
-
-
-
-
Complex I-28.5KD
-
-
-
-
Complex I-29.9KD
-
-
-
-
Complex I-29KD
-
-
-
-
Complex I-30KD
-
-
-
-
Complex I-38.5KD
-
-
-
-
Complex I-39KD
-
-
-
-
Complex I-40KD
-
-
-
-
Complex I-42.5KD
-
-
-
-
Complex I-42KD
-
-
-
-
Complex I-49KD
-
-
-
-
Complex I-51KD
-
-
-
-
Complex I-75KD
-
-
-
-
Complex I-78KD
-
-
-
-
Complex I-9.5KD
-
-
-
-
Complex I-9KD
-
-
-
-
Complex I-AGGG
-
-
-
-
Complex I-AQDQ
-
-
-
-
Complex I-ASHI
-
-
-
-
Complex I-B12
-
-
-
-
Complex I-B14
-
-
-
-
Complex I-B14.5a
-
-
-
-
Complex I-B14.5b
-
-
-
-
Complex I-B15
-
-
-
-
Complex I-B16.6
-
-
-
-
Complex I-B17
-
-
-
-
Complex I-B17.2
-
-
-
-
Complex I-B18
-
-
-
-
Complex I-B22
-
-
-
-
Complex I-B8
-
-
-
-
Complex I-B9
-
-
-
-
Complex I-KFYI
-
-
-
-
Complex I-MLRQ
-
-
-
-
Complex I-MNLL
-
-
-
-
Complex I-MWFE
-
-
-
-
Complex I-PDSW
-
-
-
-
Complex I-PGIV
-
-
-
-
Complex I-SGDH
-
-
-
-
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase
-
-
-
-
DPNH-coenzyme Q reductase
-
-
-
-
DPNH-ubiquinone reductase
-
-
-
-
electron transfer complex I
-
-
-
-
Gene associated with retinoic-interferon-induced mortality 19 protein
-
-
-
-
GGHPW
-
-
-
-
GRIM-19
-
-
-
-
Hypothetical protein Walter
-
-
-
-
Internal NADH dehydrogenase
-
-
-
-
mitochondrial electron transport complex 1
-
-
-
-
mitochondrial electron transport complex I
-
-
-
-
NADH coenzyme Q1 reductase
-
-
-
-
NADH-coenzyme Q oxidoreductase
-
-
-
-
NADH-coenzyme Q reductase
-
-
-
-
NADH-CoQ oxidoreductase
-
-
-
-
NADH-CoQ reductase
-
-
-
-
NADH-ferricyanide reductase
-
-
-
-
NADH-Q6 oxidoreductase
-
-
-
-
NADH-quinone reductase
-
-
-
-
NADH-ubiquinone oxidoreductase
-
-
-
-
NADH-ubiquinone reductase
-
-
-
-
NADH-ubiquinone-1 reductase
-
-
-
-
NADH:Q oxidoreductase
-
-
-
-
NADH:ubiquinone oxidoreductase complex
-
-
-
-
Protein P1
-
-
-
-
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase
-
-
-
-
reductase, ubiquinone
-
-
-
-
type I dehydrogenase
-
-
-
-
ubiquinone reductase
-
-
-
-
Ubiquinone-binding protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
NADH:ubiquinone oxidoreductase
The enzyme is a very large complex that participates in electron transfer chains of mitochondria and aerobic bacteria, transferring electrons from NADH to the ubiquinone pool. Reversed electron transport through this enzyme can reduce NAD+ to NADH.
CAS REGISTRY NUMBER
COMMENTARY
9028-04-0
-
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 + ubiquinone-1 + 5 H+[side 1]
NAD+ + ubiquinol-1 + 4 H+[side 2]
-
-
-
?
NADH + H+ + oxidized dichlorophenolindophenol
NAD+ + reduced dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + ubiquinone-0
NAD+ + ubiquinol-0
-
prefers ubiquinol-0 as an acceptor substrate, and can also use the artificial electron acceptors, menadione and dichlorophenolindophenol
-
-
?
additional information
?
-
-
no activity with coenzyme Q4 and coenzyme QD
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
signal shape and g values of cluster N4 [4Fe(G)C], are particularly sensitive to the changes of the environment around N4
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-fluoro-3-methyl-2-(4-(4-(trifluoromethoxy)benzyl)-phenyl)quinolin-4(1H)-one
inhibitor exhibits potency against both drug-resistant strains in vitro and parasite-infected mice in vivo via a potential allosteric mechanism. Inhibitor can be used in combination with dihydroartemisinin synergistically
additional information
-
no inhibition: dibenziodolium chloride, diphenyliodonium chloride, 1-hydroxy-2-dodecyl-4(1H)quinolone, atovaquone, antimycin A, rotenone, flavone, artemisinin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
pH 6.0: about 50% of maximal activity, pH 10.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of apoprotein an in complex with NADH and inhibitor 5-fluoro-3-methyl-2-(4-(4-(trifluoromethoxy)benzyl)-phenyl)quinolin-4(1H)-one
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Biagini, G.A.; Viriyavejakul, P.; Oneill, P.M.; Bray, P.G.; Ward, S.A.
Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria
Antimicrob. Agents Chemother.
50
1841-1851
2006
Plasmodium falciparum
Gabaldon, T.; Rainey, D.; Huynen, M.A.
Tracing the evolution of a large protein complex in the eukaryotes, NADH:ubiquinone oxidoreductase (Complex I)
J. Mol. Biol.
348
857-870
2005
Anopheles gambiae, Arabidopsis thaliana, Bos taurus, Saccharomyces cerevisiae, Caenorhabditis elegans, Candida albicans, Yarrowia lipolytica, Chlamydomonas reinhardtii, Drosophila melanogaster, Homo sapiens, Mus musculus, Neurospora crassa, Plasmodium falciparum, Schizosaccharomyces pombe, Takifugu rubripes, Cryptosporidium hominis, Encephalitozoon cuniculi, Guillardia theta
Dong, C.K.; Patel, V.; Yang, J.C.; Dvorin, J.D.; Duraisingh, M.T.; Clardy, J.; Wirth, D.F.
Type II NADH dehydrogenase of the respiratory chain of Plasmodium falciparum and its inhibitors
Bioorg. Med. Chem. Lett.
19
972-975
2009
Plasmodium falciparum
Yang, Y.; Yu, Y.; Li, X.; Li, J.; Wu, Y.; Yu, J.; Ge, J.; Huang, Z.; Jiang, L.; Rao, Y.; Yang, M.
Target elucidation by cocrystal structures of NADH-ubiquinone oxidoreductase of Plasmodium falciparum (PfNDH2) with small molecule to eliminate drug-resistant malaria
J. Med. Chem.
60
1994-2005
2017
Plasmodium falciparum (Q8I302), Plasmodium falciparum
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