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Literature summary extracted from

  • 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 (2010), Biochemistry, 49, 2973-2980.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.5.9 expressed in Escherichia coli membranes Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.5.2 benzoquinol shows noncompetitive inhibition in all conditions, it can bind to multiple enzyme forms or sites, even when either of the substrates (NADH or benzoquinone) is present at high concentrations Saccharomyces cerevisiae
1.6.5.2 additional information the product inhibition pattern expected if WrbA follows a ping pong mechanism is that the pairs NAD/BQ and NADH/BQH2 display competitive inhibition, whereas the pairs NAD/NADH and BQ/BQH2 display non-competitive inhibition Saccharomyces cerevisiae
1.6.5.2 NAD+ noncompetitive inhibition with either substrate when the other substrate is at low concentrations. At high NADH concentrations, NAD and benzoquinone are competitive, indicating they bind to a common site or sites Saccharomyces cerevisiae
1.6.5.9 aurachin analogue AC0-10 specific inhibitor Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.2 additional information
-
 additional information WrbA steady-state kinetics, overview. Initial velocity as a function of either NADH or benzoquinone concentration present one or two Michaelis-Menten phases depends on the temperature at which the enzyme is held prior to assay. The effect of temperature is reversible, suggesting an intramolecular conformational process Saccharomyces cerevisiae
1.6.5.2 14.9
-
 benzoquinone at 0.02 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 16.2
-
 NADH at 0.02 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 19
-
 NADH at 0.01 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 19
-
 benzoquinone at 0.01 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 19.3
-
 benzoquinone at 0.05 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 20.7
-
 NADH at 0.05 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 28.2
-
 NADH at 0.1 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.2 36.3
-
 benzoquinone at 0.1 mM, pH 6.0, 23°C Saccharomyces cerevisiae
1.6.5.9 0.0079
-
 ubiquinone-2 in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication Saccharomyces cerevisiae
1.6.5.9 0.0152
-
 ubiquinone-1 in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication Saccharomyces cerevisiae
1.6.5.9 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 Saccharomyces cerevisiae
1.6.5.9 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 Saccharomyces cerevisiae
1.6.5.9 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 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.9 mitochondrial membrane
-
 Saccharomyces cerevisiae 31966
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.5.9 53000
-
 estimated from amino acid sequence Saccharomyces cerevisiae

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+ + a quinone Saccharomyces cerevisiae
-
 NAD+ + a hydroquinone
-
 ?
1.6.5.2 NADPH + H+ + a quinone Saccharomyces cerevisiae
-
 NADP+ + a hydroquinone
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.2 Saccharomyces cerevisiae
-
-
-
1.6.5.9 Saccharomyces cerevisiae P32340
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.5.9 streptavidin-agarose chromatography Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
1.6.5.2 NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone ping-pong reaction mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.2 NADH + H+ + a quinone
-
 Saccharomyces cerevisiae NAD+ + a hydroquinone
-
 ?
1.6.5.2 NADH + H+ + benzoquinone
-
 Saccharomyces cerevisiae NAD+ + benzoquinol
-
 ?
1.6.5.2 NADPH + H+ + a quinone
-
 Saccharomyces cerevisiae NADP+ + a hydroquinone
-
 ?
1.6.5.2 NADPH + H+ + benzoquinone
-
 Saccharomyces cerevisiae NADP+ + benzoquinol
-
 ?
1.6.5.9 NADH + H+ + 2-azido-5-geranyl-3-methoxy-6-methyl-1,4-benzoquinone
-
 Saccharomyces cerevisiae NAD+ + 2-azido-5-geranyl-3-methoxy-6-methyl-1,4-benzoquinol
-
 ?
1.6.5.9 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
-
 Saccharomyces cerevisiae 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
-
 ?
1.6.5.9 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
-
 Saccharomyces cerevisiae 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
-
 ?
1.6.5.9 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
-
 Saccharomyces cerevisiae 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
-
 ?
1.6.5.9 NADH + H+ + ubiquinone-1
-
 Saccharomyces cerevisiae NAD+ + ubiquinol-1
-
 ?
1.6.5.9 NADH + H+ + ubiquinone-2
-
 Saccharomyces cerevisiae NAD+ + ubiquinol-2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.5.2 More dimer-tetramer assembly equilibrium documented for apoWrbA by analytical ultracentrifugation, large effect of temperature on the subunit assembly state of both apo- and holoWrbA, overview Saccharomyces cerevisiae
1.6.5.2 tetramer three subunits of the tetrameric enzyme contribute to each of four identical, cavernous active sites that appear to accommodate NAD(P)H or various quinones, but not simultaneously, suggesting an obligate tetramer with a ping-pong mechanism in which NAD departs before oxidized quinone binds Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.6.5.2 FMN-dependent NAD(P)H:quinone oxidoreductase
-
 Saccharomyces cerevisiae
1.6.5.2 WrbA
-
 Saccharomyces cerevisiae
1.6.5.9 alternative NADH-quinone oxidoreductase
-
 Saccharomyces cerevisiae
1.6.5.9 Ndi1 an NDH-2-type alternative NADH-quinone oxidoreductase Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.5.2 23
-
 assay at room temperature Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.2 6
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.2 FMN
-
 Saccharomyces cerevisiae
1.6.5.2 NADH
-
 Saccharomyces cerevisiae
1.6.5.2 NADPH
-
 Saccharomyces cerevisiae
1.6.5.9 FAD Ndi1 contains noncovalently bound FAD Saccharomyces cerevisiae
1.6.5.9 additional information Ndi1 contains no iron-sulfur cluster Saccharomyces cerevisiae
1.6.5.9 NADH
-
 Saccharomyces cerevisiae