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EC Number Reaction Commentary Reference
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.3.5.2(S)-dihydroorotate + a quinone = orotate + a quinol - -
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.3.5.2(S)-dihydroorotate + a quinone = orotate + a quinol enzyme uses a stepwise mechanism for dihydroorotate oxidation 696348
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.3.5.2(S)-dihydroorotate + a quinone = orotate + a quinol ping-pong mechanism 390918, 391223, 391226
Show all pathways known for 1.3.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.3.5.2(S)-dihydroorotate + a quinone = orotate + a quinol soluble quinones as second substrate 391223
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