4.1.1.23	5,5'-dithiobis(2-nitrobenzoate)	0.1 mM, 2.2fold stimulation	651345	
4.1.1.23	5,5'-dithiobis(2-nitrobenzoic acid)	0.1 mM, at 70°C, 2.2fold activation	651345	
4.1.1.23	6-Azauracil	1 mM, 1.2fold activation	651345	
4.1.1.23	D-erythritol 4-phosphate	activates the decarboxylation of 5-fluoroorotate. This activation is due to the utilization of binding energy from interactions between OMPDC and activator	748039	
4.1.1.23	D-glycerol 3-phosphate	activates the decarboxylation of 5-fluoroorotate.	748039	
4.1.1.23	HPO32-	decarboxylation of substrate analog 5'-deoxy-5-fluoroorotidine is activated. Decarboxylation of truncated substrate analog 1-(beta-D-erythrofuranosyl)-5-fluoroorotic acid is activated by exogenous phosphite dianion, but the 5-F substituent results in only a 0.8 kcal stabilization of the transition state for the phosphite-activated reaction	727024	
4.1.1.23	additional information	enzyme ScOMPDC-catalyzed decarboxylation of 5-fluoroorotate is stabilized by 5.2, 7.2, and 9.0 kcal/mol, respectively, by 1.0 M phosphite dianion, D-glycerol 3-phosphate and D-erythritol 4-phosphate, so that binding interactions between both the substrate phosphodianion and the ribosyl hydroxyls are utilized to activate ScOMPDC for catalysis	746572	
4.1.1.23	N-ethylmaleimide	10 mM, 18fold stimulation	651345	
4.1.1.23	N-ethylmaleimide	10 mM, at 70°C, 17.8fold activation	651345	
4.1.1.23	orotidine 5'-phosphate	the 5'-phosphate group of the substrate activates the enzyme 240000000fold. The binding of orotidine 5'-monophosphate is accompanied by a conformational change of the enzyme from an open, inactive conformation to a closed, active conformation. As the substrate traverses the reaction coordinate to form the stabilized vinyl carbanion/carbene intermediate, interactions that destabilize the carboxylate group of the substrate and stabilize the intermediate are enforced. The activation is equivalently described by an intrinsic binding energy of 11.4 kcal/mol. The residues that directly contact the 5'-phosphate group, participate in a hydrophobic cluster near the base of the active site loop that sequesters the bound substrate from the solvent, or that form hydrogen bonding interactions across the interface between the mobile and fixed half-barrel domains of the (beta/alpha)8-barrel structure. The data support a model in which the intrinsic binding energy provided by the 5'-phosphate group is used to allow interactions both near the N-terminus of the active site loop and across the domain interface that stabilize the complexes of the enzyme in the active closed conformation with the substrate or with the substrate intermediate with the destabilized carboxylate group relative to the complex of the enzyme in the open inactive conformation with the substrate	727006