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Literature summary for 1.6.5.2 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
Search for more literature for 1.6.5.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli NADH dehydrogenase knockout strain ANN0222 Plasmodium falciparum
expression in Escherichia coli Plasmodium falciparum

General Stability

General Stability Organism
not stable to repeated freeze-thaw cycles Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
1-hydroxy-2-dodecyl-4(1H)-quinolone
-
 Plasmodium falciparum
1-hydroxy-2-dodecyl-4(1H)quinolone
-
 Plasmodium falciparum
1-hydroxy-2-octyl-4(1H)quinolone
-
 Plasmodium falciparum
diphenylene iodonium chloride
-
 Plasmodium falciparum

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + atovaquone Plasmodium falciparum atovaquone is 2-[4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione NAD+ + reduced atovaquone
-
 ?
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
-
 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Storage Stability

Storage Stability Organism
-80°C, stable for at least 6 months Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H+ + atovaquone atovaquone is 2-[4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione Plasmodium falciparum NAD+ + reduced atovaquone
-
 ?
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
-
 ?
NADH + H+ + ubiquinone-1
-
 Plasmodium falciparum NAD+ + ubiquinol-1
-
 ?
NADH + H+ + ubiquinone-10
-
 Plasmodium falciparum NAD+ + ubiquinol-10
-
 ?
NADPH + H+ + ubiquinone-1
-
 Plasmodium falciparum NADP+ + ubiquinol-1
-
 ?
NADPH + H+ + ubiquinone-10
-
 Plasmodium falciparum NADP+ + ubiquinol-10
-
 ?

Synonyms

Synonyms Comment Organism
NDH2
-
 Plasmodium falciparum
PfNdh2
-
 Plasmodium falciparum
type II NADH: quinone oxidoreductase
-
 Plasmodium falciparum

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Plasmodium falciparum
NADH PfNDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
NADH NDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
NADPH PfNDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum
NADPH NDH2 can use both NADH and NADPH as electron donor Plasmodium falciparum