EC Number   |
General Information |
Reference |
|---|
   1.3.1.6 | metabolism |
the enzyme is part of the NADH-fumarate reductase system in cancer cell microenvironments, with deficiencies of critical nutrients and hypoxia, where it is important for maintaining mitochondrial energy metabolism, overview. The NADH-fumarate reductase system is the function of complex II |
710873 |
| 1.3.1.6 | more |
the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. The redox behaviour of the fumarate reductase is similar and dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV |
-, 696425 |
| 1.3.1.6 | more |
the frdA::cat strain is completely deficient in succinate dehydrogenase activity in vitro and is unable to perform whole-cell succinate-dependent respiration. The mutant strain is also unable to grow with the characteristic wild-type biphasic growth pattern and exhibits only the first growth phase, which is marked by the consumption of aspartate, serine, and associated organic acids |
-, 712285 |
| 1.3.1.6 | physiological function |
aerobic incubation of FRD with NADH results in O2 consumption. Fumarate reductase activity of FRD significantly exceeds its NADH dehydrogenase activity. During the catalysis of NADH:fumarate oxidoreductase reaction, FRD turnover is limited by a very low rate (about 10/s) of electron transfer between the noncovalently and covalently bound FMN moieties |
-, 763043 |
| 1.3.1.6 | physiological function |
complex II catalyzes the reduction of fumarate, which is the reverse of the reaction catalyzed by succinate-ubiquinone reductase, SQR, as the final step enzyme in the NADH-fumarate reductase system |
713389 |
| 1.3.1.6 | physiological function |
the increased longevity of worms provided by malate addition does not occur in fumarase fum-1, glyoxylate shunt gei-7, succinate dehydrogenase flavoprotein sdha-2, or soluble fumarate reductase F48E8.3 RNAi knockdown worms. Therefore, to increase lifespan, malate must be first converted to fumarate, then fumarate must be reduced to succinate by soluble fumarate reductase and the mitochondrial electron transport chain complex II. Fumarate reduction, glyoxylate shunt activity, and mild mitochondrial uncoupling likely contribute to the lifespan extension induced by malate and fumarate by increasing the amount of oxidized NAD and FAD cofactors |
726328 |
