1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	-	-	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	68% identity with type A enzyme of Lactococcus lactis, two-site non-classical ping-pong kinetic mechanism	390930	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	different binding sites for dihydroorotate and the electron acceptor, two-site ping-pong mechanism. Cleavage site at R182 is conserved between the two major families of dihydroorotate dehydrogenases, it is positioned in a loop, which is crucial for catalysis but irrelevant for protein stability	390918	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	enzyme uses a stepwise mechanism for dihydroorotate oxidation	696348	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	existence of 3 families differing in their selectivity for oxidizing substrates: 1A are soluble, containing FMN and use fumarate, 1B are soluble, one subunit contains an iron-sulfur center, FAD and reduces NAD+, family 2 enzymes are membrane-bound, contain FMN and are oxidized by ubiquinone. Mechanism consists of 3 reaction phases. Different binding-mechanisms for enzyme the reaction-steps are suggested	390919	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	fourth step in biosynthesis of pyrimidines. Two domains: alpha/beta-barrel domain containing the active site, one alpha-helical domain that forms the opening of a tunnel leading to active site	390920	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity	390925	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	one-site ping-pong mechanism, residues 129-137 form a flexible loop, responsible for substrate binding	390918	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	ping-pong mechanism	390918, 391223, 391226	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	soluble quinones as second substrate	391223	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	the active base S175 and the hydrogen bonding network including residues T178 and F115 work together for efficient deprotonation of dihydroorotate	696365	
1.3.5.2	(S)-dihydroorotate + a quinone = orotate + a quinol	two-site ping-pong mechanism	655559