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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485863, 485864, 485849, 485857, 485872, 485845, 485835, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485862, -
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
carbamoylphosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
485837, 485848, 485855, 485856, 485862, 485863, 485849, 485857, 485872, 485845, 485838, 485839, 485840, 485841, 485842, 485843, 485844, 485846, 485853, 485870, 485871, 485874, 485877, 485881, 485882, 485883, 485884, 485885, 1735, 485836, 485880, 485866, 485859, 485865, 485886, 485879, 485858, 485860, 485861, 1734, 485852, 485875, 485876, 485847, 485850, 485851, 485873, 485878, 485854, 485869, 485887, 485835, 485864
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
L-aspartate + carbamoyl phosphate = phosphate + N-carbamoyl-L-aspartate
-
N-carbamoyl-L-asparagine + H2O = N-carbamoyl-L-aspartate + NH3
-
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydro-DL-orotate + H2O = N-carbamoyl-L-aspartate
-
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
dihydroorotate + H2O = N-carbamoyl-L-aspartate
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-dihydroorotate + H2O = N-carbamoyl-L-aspartate
-
L-carboxymethylhydantoin + H2O = N-carbamoyl-L-aspartic acid
-
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Purification of a multifunctional protein bearing carbamyl-phosphate synthase, aspartate transcarbamylase, and dihydroorotase enzyme activities from mutant hamster cells
1978
Coleman, P.F.; Suttle, D.P.; Stark, G.R.
Methods Enzymol.
51
121-134
A multienzyme complex of carbamoyl-phosphate synthase (glutamine):aspartate carbamoyltransferase:dihydroorotase (rat ascites hepatoma cells and rat liver)
1978
Mori, M.; Tatibana, M.
Methods Enzymol.
51
111-121
-
Characterization of an extracellular asparaginase of Rhodosporidium toruloides CBS14 exhibiting unique physicochemical properties
1996
Ramakrishnan, M.S.; Joseph, R.
Can. J. Microbiol.
42
316-325
Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin
1953
Lieberman, I.; Kornberg, A.
J. Biol. Chem.
207
911-924
Microbial hydantoinases - industrial enzymes from the origin of life?
1999
Syldatk, C.; May, O.; Altenbuchner, J.; Mattes, R.; Siemann, M.
Appl. Microbiol. Biotechnol.
51
293-309
Enzyme elements involved in the interconversion of L-carbamylaspartate and L-dihydroorotate by dihydroorotase from Clostridium oroticum
1985
Pettigrew, D.W.; Mehta, B.J.; Bidigare, R.R.; Choudhuri, R.R.; Scheffler, J.F.; Sander, E.G.
Arch. Biochem. Biophys.
243
447-553
Evidence for a pH-dependent isomerization of Clostridium oroticum dihydroorotase
1985
Bidigare, R.R.; Sander, E.G.; Pettigrew, D.W.
Biochim. Biophys. Acta
831
159-160
Dihydroorotase from Escherichia coli. Purification and characterization
1984
Washabaugh, M.W.; Collins, K.D.
J. Biol. Chem.
259
3293-3298
Enzymes of pyrimidine biosynthesis in Trypanosoma cruzi
1980
Hammond, D.J.; Gutteridge W.E.
FEBS Lett.
118
259-262
Dihydroorotase from Clostridium oroticum is an allosteric enzyme
1979
Scheffler, J.E.; MA, J.; Sander E.G.
Biochem. Biophys. Res. Commun.
91
563-568
Interconvension of carbamyl-L-aspartate and L-dihydroorotate by dihydroorotase from mouse Ehrlich ascites carcinoma
1979
Christopherson, R.I.; Jones, M.E.
J. Biol. Chem.
254
12506-12512
Purification and properties of dihydroorotase, a zinc-containing metalloenzyme in Clostridium oroticum
1976
Taylor, W.H.; Taylor, M.L.; Balch, W.E.; Gilchrist, P.S.
J. Bacteriol.
127
863-873
Dihydroorotase from rat liver: purification, properties and regulatory role in pyrimidine biosynthesis
1974
Kennedy, J.
Arch. Biochem. Biophys.
160
358-365
Pyrimidine biosynthesis in parasitic protozoa: purification of a monofunctional dihydroorotase from Plasmodium berghei and Crithidia fasciculata
1990
Krungkrai, J.; Cerami, A.; Henderson, G.B.
Biochemistry
29
6270-6275
Purification and characterization of dihydroorotase from Pseudomonas putida
1995
Ogawa, J.; Shimizu, S.
Arch. Microbiol.
164
353-357
Structural and transcriptional analysis of the pyrABCN, pyrD and pyrF genes in Aspergillus nidulans and the evolutionary origin of fungal dihydroorotases
1999
Aleksenko.A.; Liu, W.; Gojkovic, Z.; Nielsen, J.; Piskur, J.
Mol. Microbiol.
33
599-611
-
Production and crystallization of aspartate transcarbamylase
1960
Sheperdson, M.; Pardee, A.B.
J. Biol. Chem.
235
3233-3237
Studies on the biosynthesis of carbamylaspartic acid
1956
Lowenstein, J.M.; Cohen, P.P.
J. Biol. Chem.
220
57-70
-
Aspartate transcarbamylases
1973
Jacobson, G.R.; Stark, G.R.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
9
225-308
Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms
1989
Allewell, N.M.
Annu. Rev. Biophys. Biophys. Chem.
18
71-92
Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition
1990
Kantrowitz, E.R.; Lipscomb, W.N.
Trends Biochem. Sci.
15
53-59
Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: binding studies using continuous-flow dialysis
1992
England, P.; Herve, G.
Biochemistry
31
9725-9732
Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits
1975
Mort, J.S.; Chan, W.W.C.
J. Biol. Chem.
250
653-660
The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites
1991
Zhang, Y.; Kantrowitz, E.R.
J. Biol. Chem.
266
22154-22158
Phosphorus-containing inhibitors of aspartate transcarbamoylase from Escherichia coli
1990
Laing, N.; Chan, W.W.C.; Hutchinson, D.W.; Íberg, B.
FEBS Lett.
260
206-208
Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway
1985
Nowlan, S.C.; Kantrowitz, E.R.
J. Biol. Chem.
260
14712-14716
N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture
1974
Swyryd, E.A.; Seaver, S.S.; Stark, G.R.
J. Biol. Chem.
249
6945-6950
Chemical stabilization of conformational states of aspartate transcarbamoylase
1987
Enns, C.A.; Chan, W.W.C.
Methods Enzymol.
135
569-577
-
Wheat-germ aspartate transcarbamoylase: potentiation of end-product inhibition in vitro by deoxycholate
1973
Yon, R.J.
Biochem. Soc. Trans.
1
676-678
Plant aspartate transcarbamylase: an affinity chromatographic method for the purification of the enzyme from germinated seedings
1979
Rao, G.S.J.; Savithri, H.S.; Seethalakshmi, S.; Rao, N.A.
Anal. Biochem.
95
401-405
Purification and properties of Bacillus subtilis aspartate transcarbamylase
1975
Brabson, J.S.; Switzer, R.L.
J. Biol. Chem.
250
8664-8669
Versatility of mixed-function adsorbents in biospecific protein desorption: accidental affinity and an improved purification of aspartate transcarbamoylase from wheat germ
1981
Yon, R.J.
Anal. Biochem.
113
219-228
Wheat-germ aspartate transcarbamoylase. Purification and cold-lability
1979
Grayson, J.E.; Yon, R.J.; Butterworth, P.J.
Biochem. J.
183
239-245
The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein, CAD
1983
Grayson, D.R.; Evans, D.R.
J. Biol. Chem.
258
4123-4129
Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions
1975
Jacobson, G.R.; Stark, G.R.
J. Biol. Chem.
250
6852-6860
Partial characterization of aspartate transcarbamylase from the mantle of the mussel Mytilus edulis
1985
Mathieu, M.
Comp. Biochem. Physiol. B
82
667-674
-
Purification and regulation of aspartate transcarbamylase from germinated mung bean (Vigna radiata) seedlings
1984
Prasad, P.V.; Rao, N.A.
J. Biosci.
6
233-248
-
Plant aspartate transcarbamylase: kinetic properies of the enzyme from mung bean (Phaseolus aureus) seedlings
1978
Savithri, H.S.; Vaidyanathan, C.S.; Rao, N.A.
Proc. Indian Acad. Sci. Sect. B
87B
81-94
Aspartate transcarbamylase from Bacillus subtilis
1985
Brabson, J.S.; Maurizi, M.R.; Switzer, R.L.
Methods Enzymol.
113
627-635
Aspartate carbamyltransferase (Streptococcus faecalis)
1978
Chang, T.Y.; Prescott, L.M.; Jones, M.E.
Methods Enzymol.
51
41-50
Aspartate carbamyltransferase (Pseudomonas fluorescens)
1978
Adair, L.B.; Jones, M.E.
Methods Enzymol.
51
51-58
Aspartate transcarbamylase from Streptococcus faecalis. Purification, properties, and nature of an allosteric activator site
1974
Chang, T.Y.; Jones, M.E.
Biochemistry
13
629-638
Aspartate transcarbamylase from Streptococcus faecalis. Steady-state kinetic analysis
1974
Chang, T.Y.; Jones, M.E.
Biochemistry
13
638-645
Studies on plant aspartate transcarbamylase. Purification and properties of the enzyme from mung-bean (Phaseolus aureus) seedlings
1974
Achar, B.S.; Savithri, H.S.; Vaidyanathan, C.S.; Rao, N.A.
Eur. J. Biochem.
47
15-22
Aspartate transcarbmoylase from Phaseolus aureus
1972
Ong, B.L.; Jackson, J.F.
Biochem. J.
129
571-581
Purification of aspartate transcarbamylase from Drosophila melanogaster
1978
Jarry, B.P.
Eur. J. Biochem.
87
533-540
Purification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens
1972
Adair, L.B.; Jones, M.E.
J. Biol. Chem.
247
2308-2315
Purification and properties of aspartate transcarbamylase from Mycobacterium smegmatis
1988
Masood, R.; Venkitasubramanian, T.A.
Biochim. Biophys. Acta
953
106-113
-
The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaeobacterium
1994
Purcarea, C.; Erauso, G.; Prieur, D.; Herve, G.
Microbiology
140
1967-1975
The activation of Escherichia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2' at the hydrophobic interface between the two domains of the regulatory chains
1994
Xi, X.G.; De Staercke, C.; Van Vliet, F.; Triniolles, F.; Jacobs, A.; Stas, P.P.; Ladjimi, M.M.; Simon, V.; Cunin, R.; Herve, G.
J. Mol. Biol.
242
139-149
Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism
1995
Lee, B.H.; Ley, B.W.; Kantrowitz, E.R.; O'Leary, M.H.; Wedler, F.C.
J. Biol. Chem.
270
15620-15627
Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis
1995
Baker, D.P.; Aucoin, J.M.; Williams, M.K.; DeMello, L.A.; Kantrowitz, E.R.
Protein Expr. Purif.
6
679-684
-
Effects of lipids on nucleotide inhibition of wheat-germ aspartate transcarbamoylase: evidence of an additional level of control?
1996
Khan, A.; Chowdhry, B.Z.; Yon, R.J.
Biochem. J.
313
669-673
Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase
1996
Yuan, X.; LiCata, V.J.; Allewell, N.M.
J. Biol. Chem.
271
1285-1294
In situ properties of Helicobacter pylori aspartate carbamoyltransferase
1997
Burns, B.P.; Mendz, G.L.; Hazell, S.L.
Arch. Biochem. Biophys.
347
119-125
-
Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: properties of the enzyme, genetic organization and synthesis in Escherichia coli
1998
Xu, Y.; Zhang, Y.; Liang, Z.; Van de Casteele, M.; Legrain, C.; Glansdorff, N.
Microbiology
144
1435-1441
Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases
1998
Liu, L.; Wales, M.E.; Wild, J.R.
J. Mol. Biol.
282
891-901
Wheat germ aspartate transcarbamoylase: revised purification, stability and re-evaluation of regulatory kinetics in terms of the Monod-Wyman-Changeux model
1999
Khan, A.I.; Chowdhry, B.Z.; Yon, R.J.
Eur. J. Biochem.
259
71-78
Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius cloning, sequence analysis, enzyme purification and characterization
1999
Durbecq, V.; Thia-Toong, T.L.; Charlier, D.; Villeret, V.; Roovers, M.; Wattiez, R.; Legrain, C.; Glansdorff, N.
Eur. J. Biochem.
264
233-241
Life-cycle-dependent changes of aspartate carbamoyltransferase localization in membranes of Saccharomyces cerevisiae - centrifugal elutriation and ultracytochemical study
1999
Vorisek, J.; Noaillac-Depeyre, J.; Denis-Duphil, M.
Folia Microbiol. (Praha)
44
289-294
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1.ANG
1999
Jin, L.; Stec, B.; Lipscomb, W.N.; Kantrowitz, E.R.
Proteins Struct. Funct. Genet.
37
729-742
Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii
2000
Hack, E.S.; Vorobyova, T.; Sakash, J.B.; West, J.M.; Macol, C.P.; Herve, G.; Williams, M.K.; Kantrowitz, E.R.
J. Biol. Chem.
275
15820-15827
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation
2000
Endrizzi, J.A.; Beernink, P.T.; Alber, T.; Schachman, H.K.
Proc. Natl. Acad. Sci. USA
97
5077-5082
Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase
2002
Fetler, L.; Tauc, P.; Baker, D.P.; Macol, C.P.; Kantrowitz, E.R.; Vachette, P.
Protein Sci.
11
1074-1081
Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation
2002
West, J.M.; Tsuruta, H.; Kantrowitz, E.R.
J. Biol. Chem.
277
47300-47304
Pseudomonas aeruginosa aspartate transcarbamoylase. Characterization of its catalytic and regulatory properties
2002
Vickrey, J.F.; Herve, G.; Evans, D.R.
J. Biol. Chem.
277
24490-24498
Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8 A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate
2003
Van Boxstael, S.; Cunin, R.; Khan, S.; Maes, D.
J. Mol. Biol.
326
203-216
Dihydroorotase catalyzes the ring opening of the hydrolysis intermediates of the cardioprotective drug dexrazoxane (ICRF-187)
2002
Schroeder, P.E.; Davidson, J.N.; Hasinoff, B.B.
Drug Metab. Dispos.
30
1431-1435
Aquifex aeolicus dihydroorotase: association with aspartate transcarbamoylase switches on catalytic activity
2004
Ahuja, A.; Purcarea, C.; Ebert, R.; Sadecki, S.; Guy, H.I.; Evans, D.R.
J. Biol. Chem.
279
53136-53144
Mechanism of the dihydroorotase reaction
2004
Porter, T.N.; Li, Y.; Raushel, F.M.
Biochemistry
43
16285-16292
13C and 15N isotope effects for conversion of L-dihydroorotate to N-carbamyl-L-aspartate using dihydroorotase from hamster and Bacillus caldolyticus
2006
Anderson, M.A.; Cleland, W.W.; Huang, D.T.; Chan, C.; Shojaei, M.; Christopherson, R.I.
Biochemistry
45
7132-7139
Thermodynamic analysis of catalysis by the dihydroorotases from hamster and Bacillus caldolyticus, as compared with the uncatalyzed reaction
2006
Huang, D.T.; Kaplan, J.; Menz, R.I.; Katis, V.L.; Wake, R.G.; Zhao, F.; Wolfenden, R.; Christopherson, R.I.
Biochemistry
45
8275-8283
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits
2005
Lee, M.; Chan, C.W.; Mitchell Guss, J.; Christopherson, R.I.; Maher, M.J.
J. Mol. Biol.
348
523-533
Cloning and preliminary characterization of the dihydroorotase from Toxoplasma gondii
2006
Robles Lopez, S.M.; Hortua Triana, M.A.; Zimmermann, B.H.
Mol. Biochem. Parasitol.
148
93-98
Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibitor 5-fluoroorotate: catalytic activity is reflected by the crystal form
2007
Lee, M.; Maher, M.J.; Guss, J.M.
Acta Crystallogr. Sect. F
F63
154-161
Dihydroorotase of human malarial parasite Plasmodium falciparum differs from host enzyme
2008
Krungkrai, S.R.; Wutipraditkul, N.; Krungkrai, J.
Biochem. Biophys. Res. Commun.
366
821-826
Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state
2007
Lee, M.; Maher, M.J.; Christopherson, R.I.; Guss, J.M.
Biochemistry
46
10538-10550
Structures of ligand-free and inhibitor complexes of dihydroorotase from Escherichia coli: implications for loop movement in inhibitor design
2007
Lee, M.; Chan, C.W.; Graham, S.C.; Christopherson, R.I.; Guss, J.M.; Maher, M.J.
J. Mol. Biol.
370
812-825
Dihydroorotase from the hyperthermophile Aquifex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis
2009
Zhang, P.; Martin, P.D.; Purcarea, C.; Vaishnav, A.; Brunzelle, J.S.; Fernando, R.; Guy-Evans, H.I.; Evans, D.R.; Edwards, B.F.
Biochemistry
48
766-778
High-level expression, purification, and characterization of Staphylococcus aureus dihydroorotase (PyrC) as a cleavable His-SUMO fusion
2013
Truong, L.; Hevener, K.E.; Rice, A.J.; Patel, K.; Johnson, M.E.; Lee, H.
Protein Expr. Purif.
88
98-106
Biochemical characterization of dihydroorotase of Leishmania donovani understanding pyrimidine metabolism through its inhibition
2016
Tiwari, K.; Kumar, R.; Dubey, V.K.
Biochimie
131
45-53
Biochemical characterization of dihydroorotase of Leishmania donovani understanding pyrimidine metabolism through its inhibition
2016
Tiwari, K.; Kumar, R.; Dubey, V.K.
Biochimie
131
45-53
Ca-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase)
2016
Rice, A.J.; Lei, H.; Santarsiero, B.D.; Lee, H.; Johnson, M.E.
Bioorg. Med. Chem.
24
4536-4543
Ca-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase)
2016
Rice, A.J.; Lei, H.; Santarsiero, B.D.; Lee, H.; Johnson, M.E.
Bioorg. Med. Chem.
24
4536-4543
Pyrimidine biosynthesis in pathogens - structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae
2019
Lipowska, J.; Miks, C.D.; Kwon, K.; Shuvalova, L.; Zheng, H.; Lewinski, K.; Cooper, D.R.; Shabalin, I.G.; Minor, W.
Int. J. Biol. Macromol.
136
1176-1187
Pyrimidine biosynthesis in pathogens - structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae
2019
Lipowska, J.; Miks, C.D.; Kwon, K.; Shuvalova, L.; Zheng, H.; Lewinski, K.; Cooper, D.R.; Shabalin, I.G.; Minor, W.
Int. J. Biol. Macromol.
136
1176-1187
Activation of latent dihydroorotase from Aquifex aeolicus by pressure
2017
Herve, G.; Evans, H.G.; Fernado, R.; Patel, C.; Hachem, F.; Evans, D.R.
J. Biol. Chem.
292
629-637
Activation of latent dihydroorotase from Aquifex aeolicus by pressure
2017
Herve, G.; Evans, H.G.; Fernado, R.; Patel, C.; Hachem, F.; Evans, D.R.
J. Biol. Chem.
292
629-637
Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD
2018
Del Cano-Ochoa, F.; Grande-Garcia, A.; Reverte-Lopez, M.; DAbramo, M.; Ramon-Maiques, S.
J. Biol. Chem.
293
18903-18913
Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD
2018
Del Cano-Ochoa, F.; Grande-Garcia, A.; Reverte-Lopez, M.; DAbramo, M.; Ramon-Maiques, S.
J. Biol. Chem.
293
18903-18913
Characterization of the dihydroorotase from Methanococcus jannaschii
2017
Vitali, J.; Singh, A.K.; Colaneri, M.J.
Protein J.
36
361-373
Characterization of the dihydroorotase from Methanococcus jannaschii
2017
Vitali, J.; Singh, A.K.; Colaneri, M.J.
Protein J.
36
361-373
Functional analyses of Toxoplasma gondii dihydroorotase reveal a promising anti-parasitic target
2024
Pan, M.; Ge, C.C.; Niu, S.Z.; Duan, Y.Y.; Fan, Y.M.; Jin, Q.W.; Chen, X.; Tao, J.P.; Huang, S.Y.
FASEB J.
38
e23397
Identification of small molecule inhibitors against Staphylococcus aureus dihydroorotase via HTS
2021
Rice, A.J.; Pesavento, R.P.; Ren, J.; Youn, I.; Kwon, Y.; Ellepola, K.; Che, C.T.; Johnson, M.E.; Lee, H.
Int. J. Mol. Sci.
22
9984
Crystal structure of Methanococcus jannaschii dihydroorotase
2023
Vitali, J.; Nix, J.C.; Newman, H.E.; Colaneri, M.J.
Proteins
91
91-98