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Literature summary for 1.6.5.2 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
Search for more literature for 1.6.5.2

Inhibitors

Inhibitors Comment Organism Structure
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
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
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
14.9
-
 benzoquinone at 0.02 mM, pH 6.0, 23°C Saccharomyces cerevisiae
16.2
-
 NADH at 0.02 mM, pH 6.0, 23°C Saccharomyces cerevisiae
19
-
 NADH at 0.01 mM, pH 6.0, 23°C Saccharomyces cerevisiae
19
-
 benzoquinone at 0.01 mM, pH 6.0, 23°C Saccharomyces cerevisiae
19.3
-
 benzoquinone at 0.05 mM, pH 6.0, 23°C Saccharomyces cerevisiae
20.7
-
 NADH at 0.05 mM, pH 6.0, 23°C Saccharomyces cerevisiae
28.2
-
 NADH at 0.1 mM, pH 6.0, 23°C Saccharomyces cerevisiae
36.3
-
 benzoquinone at 0.1 mM, pH 6.0, 23°C Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + a quinone Saccharomyces cerevisiae
-
 NAD+ + a hydroquinone
-
 ?
NADPH + H+ + a quinone Saccharomyces cerevisiae
-
 NADP+ + a hydroquinone
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H+ + a quinone
-
 Saccharomyces cerevisiae NAD+ + a hydroquinone
-
 ?
NADH + H+ + benzoquinone
-
 Saccharomyces cerevisiae NAD+ + benzoquinol
-
 ?
NADPH + H+ + a quinone
-
 Saccharomyces cerevisiae NADP+ + a hydroquinone
-
 ?
NADPH + H+ + benzoquinone
-
 Saccharomyces cerevisiae NADP+ + benzoquinol
-
 ?

Subunits

Subunits Comment Organism
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
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

Synonyms Comment Organism
FMN-dependent NAD(P)H:quinone oxidoreductase
-
 Saccharomyces cerevisiae
WrbA
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Saccharomyces cerevisiae
NADH
-
 Saccharomyces cerevisiae
NADPH
-
 Saccharomyces cerevisiae