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EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
1.6.5.2
-999
-
more
Michaelis-Menten kinetics and first-order rate constants with NADH and quinone substrates, overview
724356
1.6.5.2
-999
-
more
steady-state kinetic analysis of the quinone reductase activity
680629
1.6.5.2
-999
-
more
steady-state kinetics, stopped-flow spectrophotometry
743659
1.6.5.2
-999
-
more
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
714189
1.6.5.2
0.0000017
-
FAD
hydrophobic isoform
394364
1.6.5.2
0.0000027
-
FAD
hydrophilic isoform
394364
1.6.5.2
0.000188
-
menadione
cofactor NADH
394383
1.6.5.2
0.00024
-
menadione
cofactor NADPH
394383
1.6.5.2
0.000437
-
naphthoquinone
cofactor NADH
394383
1.6.5.2
0.00059
-
naphthoquinone
cofactor NADPH
394383
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