orotidine-5'-monophosphate decarboxylase
Dependence of the catalytic activities on the aggregation and conformation states of uridine 5'-phosphate synthase.
Dependence of the aggregation and conformation states of uridine 5'-phosphate synthase on pyrimidine nucleotides. Evidence for a regulatory site.
Orotidine-5'-monophosphate decarboxylase catalysis: kinetic isotope effects and the state of hybridization of a bound transition-state analogue.
Crystallization of yeast orotidine 5'-monophosphate decarboxylase complexed with 1-(5'-phospho-beta-D-ribofuranosyl) barbituric acid.
Orotidylate decarboxylase: insights into the catalytic mechanism from substrate specificity studies.
A unique catalytic and inhibitor-binding role for Lys93 of yeast orotidylate decarboxylase.
Orotidylate decarboxylase of yeast and man.
Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase.
A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase.
No metal cofactor in orotidine 5'-monophosphate decarboxylase.
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5'-phosphate decarboxylase.
Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation.
Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects.
Remarkable rate enhancement of orotidine 5'-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization.
The structural basis for the remarkable catalytic proficiency of orotidine 5'-monophosphate decarboxylase.
The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog.
Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase.
Selenomethionine substitution of orotidine-5'-monophosphate decarboxylase causes a change in crystal contacts and space group.
Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization?
A reexamination of the substrate utilization of 2-thioorotidine-5'-monophosphate by yeast orotidine-5'-monophosphate decarboxylase.
Crystal structures of orotidine monophosphate decarboxylase: does the structure reveal the mechanism of nature's most proficient enzyme?
An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase.
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
Catalytic proficiency: the unusual case of OMP decarboxylase.
Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase.
Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography.
The gas phase proton affinity of uracil: measuring multiple basic sites and implications for the enzyme mechanism of orotidine 5'-monophosphate decarboxylase.
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase.
Hydrogen isotope tracing in the reaction of orotidine-5'-monophosphate decarboxylase.