1.3.98.1	K213E	decrease in activity against dichlorophenolindophenol	656148	
1.3.98.1	K296A	disturbance of intermolecular salt bridge, mutant retains almost complete activity	657291	
1.3.98.1	K296E	disturbance of intermolecular salt bridge, mutant activity is severely impaired	657291	
1.3.98.1	L71F	reaction is somehow slower than for wild-type, binding of dihydroorotate is much tighter than with wild-type	724305	
1.3.98.1	L71F/C130S/V133T	addition of the two residues comprising the conserved proton-transfer network of Class 2 dihydroorotate dehydrogenase from Escherichia coli to the C130S Class 1A enzyme of Lactococcus lacits. Mutation does not did not restore the function of the active site base or rapid flavin reduction. Kd for dihydroorotate is about three times tighter than the wild-type	724305	
1.3.98.1	L71F/V133T	reaction is drastically slower forwith wild-type, Kd for dihydroorotate is iabout eight-fold tighter than the wild-type	724305	
1.3.98.1	additional information	deletions of N-terminal residues from 2 down to 40 result in generally unstable proteins with apo protein quickly precipitating and FMN remaining in solution. A truncated protein lacking residues 2 to 30 is sufficiently stable, has near to wild-type activity using molecular oxygen and 20fold lower activity using 2,6-dichlorophenolindophenol as electron acceptor	657355	
1.3.98.1	additional information	DHOD-knockout Trypanosoma cruzi do not express the enzyme protein and can not survive even in the presence of pyrimidine nucleosides, suggesting a vital role of fumarate reductase activity in the regulation of cellular redox balance	675478	
1.3.98.1	N127A	reduced activity	656148	
1.3.98.1	N193A	drastically reduced activiy	656148