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Literature summary extracted from

  • Fisher, N.; Warman, A.J.; Ward, S.A.; Biagini, G.A.
    Type II NADH:quinone oxidoreductases of Plasmodium falciparum and Mycobacterium tuberculosis kinetic and high-throughput assays (2009), Methods Enzymol., 456, 303-320.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.5.2 expressed in Escherichia coli NADH dehydrogenase knockout strain ANN0222 Plasmodium falciparum
1.6.5.2 expression in Escherichia coli Plasmodium falciparum
7.1.1.2 expression in Escherichia coli Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
1.6.5.2 not stable to repeated freeze-thaw cycles Plasmodium falciparum
7.1.1.2 not stable to repeated freeze-thaw cycles Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.5.2 1-hydroxy-2-dodecyl-4(1H)-quinolone
-
 Plasmodium falciparum
1.6.5.2 1-hydroxy-2-dodecyl-4(1H)quinolone
-
 Plasmodium falciparum
1.6.5.2 1-hydroxy-2-octyl-4(1H)quinolone
-
 Plasmodium falciparum
1.6.5.2 diphenylene iodonium chloride
-
 Plasmodium falciparum
7.1.1.2 1-hydroxy-2-octyl-4(1H)quinolone
-
 Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.2 0.0051
-
 NADH cosubstrate: decylubiquinone Plasmodium falciparum
1.6.5.2 0.0167
-
 NADH cosubstrate: ubiquinone-1 Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.2 membrane the membrane-bound respiratory enzymes differs from the canonical NADH: dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. The enzyme possesses an amphipathic alpha-helix, which is likely to anchor the enzyme into the lipid bilayer Plasmodium falciparum 16020
-
7.1.1.2 membrane the membrane-bound respiratory enzymes differs from the canonical NADH: dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes Mycobacterium tuberculosis 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.5.2 NADH + H+ + atovaquone Plasmodium falciparum atovaquone is 2-[4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione NAD+ + reduced atovaquone
-
 ?
1.6.5.2 NADH + H+ + ubiquinone Plasmodium falciparum the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Plasmodium falciparum is the causative agents of malaria). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. In the electron transport chain of Plasmodium, the canonical multimeric complex I (NADH:dehydrogenase) found in mammalian mitochondria is absent, and, instead, the parasite possesses five quinone-dependent oxidoreductases, namely a type II NADH:quinone oxidoreductase (PfNDH2), a malate: quinone oxidoreductase (MQO), a dihydroorotate dehydrogenase (DHOD), a glycerol-3-phosphate dehydrogenase (G3PDH), and a succinate: quinone oxidoreductase (SDH). These enzymes link cytosolic metabolism to mitochondrial metabolism, generating reducing power (ubiquinol) for the bc1 complex and an aa3-type cytochrome oxidase, enabling proton pumping and energy conservation NAD+ + ubiquinone
-
 ?
7.1.1.2 NADH + H+ + menaquinone Mycobacterium tuberculosis the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Mycobacterium tuberculosis is the causative agents of tuberculosis). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. Mycobacterium tuberculosis contains a branched respiratory chain terminating in a cytochrome bd (quinol) oxidase and an aa3-type cytochrome c oxidase. Both chains are fed by a menaquinol (MQH2) pool that is generated by four dehydrogenases; one succinate menaquinone oxidoreductase (SQR), one multimeric type I NADH: dehydrogenase (complex I), and two type II NADH: menaquinone oxidoreductases (ndh and ndhA). Transposon insertion knockout strategy reveals that disruption of the ndh gene is lethal NAD+ + menaquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.2 Plasmodium falciparum
-
-
-
7.1.1.2 Mycobacterium tuberculosis
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.6.5.2 -80°C, stable for at least 6 months Plasmodium falciparum
7.1.1.2 -80°C, stable for at least 6 months Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.2 NADH + H+ + atovaquone atovaquone is 2-[4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione Plasmodium falciparum NAD+ + reduced atovaquone
-
 ?
1.6.5.2 NADH + H+ + ubiquinone the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Plasmodium falciparum is the causative agents of malaria). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. In the electron transport chain of Plasmodium, the canonical multimeric complex I (NADH:dehydrogenase) found in mammalian mitochondria is absent, and, instead, the parasite possesses five quinone-dependent oxidoreductases, namely a type II NADH:quinone oxidoreductase (PfNDH2), a malate: quinone oxidoreductase (MQO), a dihydroorotate dehydrogenase (DHOD), a glycerol-3-phosphate dehydrogenase (G3PDH), and a succinate: quinone oxidoreductase (SDH). These enzymes link cytosolic metabolism to mitochondrial metabolism, generating reducing power (ubiquinol) for the bc1 complex and an aa3-type cytochrome oxidase, enabling proton pumping and energy conservation Plasmodium falciparum NAD+ + ubiquinone
-
 ?
1.6.5.2 NADH + H+ + ubiquinone-1
-
 Plasmodium falciparum NAD+ + ubiquinol-1
-
 ?
1.6.5.2 NADH + H+ + ubiquinone-10
-
 Plasmodium falciparum NAD+ + ubiquinol-10
-
 ?
1.6.5.2 NADPH + H+ + ubiquinone-1
-
 Plasmodium falciparum NADP+ + ubiquinol-1
-
 ?
1.6.5.2 NADPH + H+ + ubiquinone-10
-
 Plasmodium falciparum NADP+ + ubiquinol-10
-
 ?
7.1.1.2 NADH + H+ + decylubiquinone the enzyme is selective for NADH Mycobacterium tuberculosis NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + H+ + menaquinone the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Mycobacterium tuberculosis is the causative agents of tuberculosis). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. Mycobacterium tuberculosis contains a branched respiratory chain terminating in a cytochrome bd (quinol) oxidase and an aa3-type cytochrome c oxidase. Both chains are fed by a menaquinol (MQH2) pool that is generated by four dehydrogenases; one succinate menaquinone oxidoreductase (SQR), one multimeric type I NADH: dehydrogenase (complex I), and two type II NADH: menaquinone oxidoreductases (ndh and ndhA). Transposon insertion knockout strategy reveals that disruption of the ndh gene is lethal Mycobacterium tuberculosis NAD+ + menaquinol
-
 ?
7.1.1.2 NADH + H+ + ubiquinone-1
-
 Mycobacterium tuberculosis NAD+ + ubiquinol-1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.6.5.2 NDH2
-
 Plasmodium falciparum
1.6.5.2 PfNdh2
-
 Plasmodium falciparum
1.6.5.2 type II NADH: quinone oxidoreductase
-
 Plasmodium falciparum
7.1.1.2 NADH:ubiquinone oxidoreductase
-
 Mycobacterium tuberculosis
7.1.1.2 NDH
-
 Mycobacterium tuberculosis
7.1.1.2 Ndh/NdhA–type II NADH:(mena)quinone oxidoreductase
-
 Mycobacterium tuberculosis
7.1.1.2 type II NADH:quinone oxidoreductase
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.2 7.5
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.2 FAD
-
 Plasmodium falciparum
1.6.5.2 NADH PfNDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
1.6.5.2 NADH NDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
1.6.5.2 NADPH PfNDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
1.6.5.2 NADPH NDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
7.1.1.2 NADH the enzyme is selective for NADH Mycobacterium tuberculosis