Enzymes
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- Name help_outline (S)-dihydroorotate Identifier CHEBI:30864 Charge -1 Formula C5H5N2O4 InChIKeyhelp_outline UFIVEPVSAGBUSI-REOHCLBHSA-M SMILEShelp_outline [O-]C(=O)[C@@H]1CC(=O)NC(=O)N1 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,285 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,279 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline orotate Identifier CHEBI:30839 (Beilstein: 3651747; CAS: 73-97-2) help_outline Charge -1 Formula C5H3N2O4 InChIKeyhelp_outline PXQPEWDEAKTCGB-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)c1cc(=O)[nH]c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:14861 | RHEA:14862 | RHEA:14863 | RHEA:14864 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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More general form(s) of this reaction
Publications
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Properties of triphosphopyridine nucleotide-linked dihydroorotic dehydrogenase.
UDAKA S., VENNESLAND B.
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Two functionally different dihydroorotic dehydrogenases in bacteria.
Taylor W.H., Taylor M.L., Eames D.F.
Taylor, W. H. (Portland State College, Portland, Ore.), M. L. Taylor, and D. F. Eames. Two functionally different dihydroorotic dehydrogenases in bacteria. J. Bacteriol. 91:2251-2256. 1966.-We have investigated the relationship between the two kinds of dihydroorotic dehydrogenases produced by bact ... >> More
Taylor, W. H. (Portland State College, Portland, Ore.), M. L. Taylor, and D. F. Eames. Two functionally different dihydroorotic dehydrogenases in bacteria. J. Bacteriol. 91:2251-2256. 1966.-We have investigated the relationship between the two kinds of dihydroorotic dehydrogenases produced by bacteria. A pseudomonad, capable of growth on a salts medium with glucose, aspartate, glycerol, or orotate as the carbon source, was isolated from lake bank mud. A particle-bound dihydroorotic dehydrogenase, similar to the biosynthetic enzyme in Escherichia coli, was formed by the pseudomonad when the carbon source was orotate, glucose, glycerol, or aspartate. A soluble, degradative nicotinamide adenine dinucleotide phosphate-linked dihydroorotic dehydrogenase, as well as the particle-bound biosynthetic enzyme, was formed when the pseudomonad was cultivated on orotate. The biosynthetic enzyme links to oxygen or ferricyanide, but not to pyridine nucleotides. Zymobacterium oroticum, when cultivated on glucose, contained only the biosynthetic type of dihydroorotic dehydrogenase. The presence of two functionally different dihydroorotic dehydrogenases in the pseudomonad was suggested on the basis of the following observations: (i) the two enzyme activities were separated by centrifugation; (ii) the pyridine nucleotide-linked activity was formed only when orotate was present in the growth medium; and (iii) the biosynthetic enzyme was stable to storage at -20 C for 4 months, whereas the degradative enzyme activity was destroyed by storage under these conditions. << Less