EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.3.5.1 | -999 |
- |
fumarate |
with menaquinone EC 1.3.5.4, succinate oxidation: 0.003 mM, pH 7.8, 30°C |
654820 |
| 1.3.5.1 | -999 |
- |
more |
interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures |
726316 |
| 1.3.5.1 | -999 |
- |
more |
midpoint potentials of [3Fe-4S] cluster and heme b, kinetics and kinetic isotope effects of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview |
685281 |
| 1.3.5.1 | -999 |
- |
more |
no effect of phosphate on fumarate reductase, but increase of Km of succinate dehydrogenase |
391169 |
| 1.3.5.1 | -999 |
- |
more |
steady-state kinetic measurements show that the enzyme displays standard Michaelis-Menten kinetics at a low temperature of 30°C but exhibits deviation from it at a higher temperature of 70°C, the enzyme shows positive cooperativity at higher temperatures |
724421 |
| 1.3.5.1 | -999 |
- |
more |
succinate-quinone and quinol-fumarate reductase reaction of succinate dehydrogenase and fumarate reductase |
391137 |
| 1.3.5.1 | -999 |
- |
succinate |
fumarate reduction. 0.0013 mM, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1 |
654820 |
| 1.3.5.1 | 0.00017 |
- |
ubiquinone-2 |
differences in Km value (9fold) and Vmax/Km ratio (19fold) between Q1 and Q2 indicate that the 6-polyprenyl tail of the ubiquinone ring contributes to the binding affinity and that Q2 is better substrate than Q1 |
698658 |
| 1.3.5.1 | 0.0005 |
- |
ubiquinone |
mutant R81E, pH 8.0, 30°C |
742846 |
| 1.3.5.1 | 0.0005 |
- |
ubiquinone-2 |
- |
391123 |
