1.3.98.1	C130A	low activity with dihydroorotate, increasing activity above pH 8.0 with dihydrooxonate	390913	
1.3.98.1	C130A	the mutant enzyme exhibits binding affinities for dihydroorotate similar to that of the wild type enzyme, reduction is extremely slow compared to that of the wild type, the rate of reduction increases with pH showing no sign of a plateau	685146	
1.3.98.1	C130A	the mutant forms charge-transfer complexes upon binding 3,4-dihydroxybenzoate, but the maximum of the broad charge-transfer bands is shifted to 590 nm	685158	
1.3.98.1	C130S	the mutant enzyme exhibits binding affinities for dihydroorotate similar to that of the wild type enzyme, reduction is extremely slow compared to that of the wild type, the rate of reduction increases with pH showing no sign of a plateau	685146	
1.3.98.1	C130S	the mutant forms charge-transfer complexes upon binding 3,4-dihydroxybenzoate, but the maximum of the broad charge-transfer bands is shifted to 610 nm	685158	
1.3.98.1	E206/K296E	conversion of intermolecular salt bridge, mutant is fully active in concentrated solutions and dissociates into monomers upon dilution like wild-type enzyme	657291	
1.3.98.1	E206A	disturbance of intermolecular salt bridge, mutant retains almost complete activity	657291	
1.3.98.1	E206K	disturbance of intermolecular salt bridge, mutant activity is severely impaired	657291	
1.3.98.1	H185A	4fold increase in KM-value of CoQD, 50% increase in KM-value of L-dihydroorotate	656285	
1.3.98.1	K136E	little changes in activity	656148