Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(beta-D-erythrofuranosyl)-5-fluoroorotate
1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
1-(beta-D-erythrofuranosyl)-5-fluoroorotic acid
1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
-
truncated analog of the natural substrate orotidine 5'-monophosphate with enhanced reactivity towards decarboxylation. The vinyl carbanion-like transition state is stabilized by 3.5 kcal/mol by interactions with the 5-F substituent. Decarboxylation 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
-
-
?
1-(beta-D-erythrofuranosyl)-orotate
1-(beta-D-erythrofuranosyl)uracil + CO2
1-(beta-D-erythrofuranosyl)orotic acid
1-(beta-D-erythrofuranosyl)uracil + CO2
-
truncated substrate
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
5'-deoxy-5-fluoroorotidine
? + CO2
-
truncated analog of the natural substrate orotidine 5'-monophosphate with enhanced reactivity towards decarboxylation. The 4'-CH3 and 4'-CH2OH groups of 5'-deoxy-5-fluoroorotidine and orotidine, respectively, result in identical destabilizations of the transition state for the unactivated decarboxylation of 2.9 kcal/mol. By contrast, the 4'-CH3 group of 5'-deoxy-5-fluoroorotidine and the 4'-CH2OH group of orotidine result in very different 4.7 and 8.3 kcal/mol destabilizations of the transition state for the phosphite-activated decarboxylation
-
-
?
5-Azaorotidine 5'-phosphate
5-Azauridine 5'-phosphate + CO2
-
-
-
-
?
5-fluoroorotate
5-fluorouracil + CO2
5-fluoroorotidine 5'-phosphate
5-fluoro-UMP + CO2
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
6-cyano-UMP + H2O
barbiturate ribonucleoside 5'-monophosphate + CN-
-
-
-
-
?
6-cyano-UMP + H2O
beta-D-ribofuranosylbarbiturate 5'-monophosphate + CN-
-
hydrolysis
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
orotate
uracil + CO2
-
-
-
?
orotic acid
?
extremely poor substrate
-
?
orotidine
uridine + CO2
-
low decarboxylation activity
-
-
?
Orotidine 5'-phosphate
UMP + CO2
orotidine 5'-phosphate + H+
UMP + CO2
additional information
?
-
1-(beta-D-erythrofuranosyl)-5-fluoroorotate
1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
-
-
-
?
1-(beta-D-erythrofuranosyl)-5-fluoroorotate
1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
-
-
-
?
1-(beta-D-erythrofuranosyl)-orotate
1-(beta-D-erythrofuranosyl)uracil + CO2
-
-
-
?
1-(beta-D-erythrofuranosyl)-orotate
1-(beta-D-erythrofuranosyl)uracil + CO2
-
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
-
decreased catalytic rate compared with orotidine 5'-phosphate as substrate
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
-
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
-
-
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
less effective than orotidine 5-phosphate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
partially active substrate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
50% reduced kcat-value compared with orotidine 5'-phosphate as substrate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
-
-
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
nearly equally effective as orotidine 5'-phosphate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
nearly equally effective as orotidine 5'-phosphate
-
?
5-fluoroorotate
5-fluorouracil + CO2
-
-
-
?
5-fluoroorotate
5-fluorouracil + CO2
-
-
-
?
5-fluoroorotidine 5'-phosphate
5-fluoro-UMP + CO2
-
-
-
?
5-fluoroorotidine 5'-phosphate
5-fluoro-UMP + CO2
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
-
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
-
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
-
the 5-fluoro substituent results in a 3400fold increase in the first-order rate constant for deuterium exchange
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
-
pseudohydrolysis process
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
-
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
pseudohydrolysis process
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
-
pseudohydrolysis process
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
-
pseudohydrolysis process
-
-
?
Orotidine 5'-phosphate
?
-
required for the biosynthesis of uridylic acid
-
-
?
Orotidine 5'-phosphate
?
-
final step in pyrimidine biosynthesis
-
-
?
Orotidine 5'-phosphate
?
-
final step in pyrimidine biosynthesis
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
catalytic mechanism, bimolecular electrophilic substitution mechanism in which decarboxylation and carbon-carbon bond protonation by Lys-62 occur in a concerted action, enzyme/active site structure, one active site per monomer, located near the dimer interface
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, enzyme structure
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechansim, no formation of a vinyl anion intermediate, enzyme structure, the active sites are located at the dimer interface
-
?
Orotidine 5'-phosphate
UMP + CO2
catalyzes the final step in the de novo biosynthesis of uridine monophosphate
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
?
Orotidine 5'-phosphate
UMP + CO2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
?
Orotidine 5'-phosphate
UMP + CO2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic mechanism, role of Lys-93 in catalysis, enzyme structure
-
?
Orotidine 5'-phosphate
UMP + CO2
-
enzyme/active site structure, contains two independently functioning active sites, binding of the phosphoryl group of the substrate is essential for the catalytic function, induced fit mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, enzyme structure
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the last step in the de novo synthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
-
last step in the de novo synthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
UMP synthase is a bifunctional enzyme that catalyzes the penultimate and last steps in the de novo biosynthesis of UMP, the bifunctional enzyme combines the orotate phosphoribosyltransferase and the orotidine-5'-monophosphate decarboxylase activities on a single polypeptide chain
-
-
?
Orotidine 5'-phosphate
UMP + CO2
the decarboxylase shows an extremely fast rate acceleration
-
-
?
Orotidine 5'-phosphate
UMP + CO2
Methanobacterium thermoautotrophicus
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
Methanobacterium thermoautotrophicus DSM 1053
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
Methanococcus thermoautotrophicum
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic mechanism, the remarkable catalytic power is almost exclusively achieved via ground state destabilization of the reactive part of substrate, which is compensated for by strong binding of the phosphate and ribose groups, and to a lesser extend via transition state stabilization, enzyme/active site structure, mode of substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism involving an equilibrium pre-protonation of orotidine 5'-phosphate C5 by the catalytic Lys-72 residue that greatly reduces the barrier to subsequent decarboxylation, Lys-72 is not critical for substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, enzyme conformation is more distorted in the reactant state than in the transition state, the energy released from conformation relaxation provides the predominant contribution to the rate enhancement, the active site consists of a network of charged residues Lys-42, Asp-70, Lys-72, Asp-75b
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, Lys-42, Asp-70, Lys-72 and Asp-75b form an alternate charged network around the reactive part of substrate, Lys-72 protonates the intermediate C6 carbanion
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the final step in the de novo biosynthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the last step of de novo pyrimidine synthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
last step in the biosynthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the enzyme catalyzes the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates, active site residues in ODCase are involved in an extensive hydrogen-bonding network, active site Lys42
-
-
?
Orotidine 5'-phosphate
UMP + CO2
the remote 5'-phosphate group of the substrate activates the enzyme 240 millionfold, the activation corresponds to an intrinsic binding energy of 11.4 kcal/mol. This intrinsic binding energy is used to allow interactions both near the N-terminus of the active site loop and across the domain interface that stabilize both the Ec-S and Ec-S* complexes relative to the Eo-S complex
-
-
?
Orotidine 5'-phosphate
UMP + CO2
the remote 5'-phosphate group of the substrate activates the enzyme 240 millionfold, the activation corresponds to an intrinsic binding energy of 11.4 kcal/mol. This intrinsic binding energy is used to allow interactions both near the N-terminus of the active site loop and across the domain interface that stabilize both the Ec-S and Ec-S* complexes relative to the Eo-S complex
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
absolutely specific
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the sixth enzyme in the pathway catalyzing formation of uridine 5'-monophosphate
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
final step in the de novo synthesis of uridine 5'-monophosphate, UMP, defects in the enzyme are lethal in the malaria parasite
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
change in active-site structure upon binding of orotidine 5'-phosphate/UMP, the backbone amide of Arg294 interacts directly with the phosphate group of the ligands, rearrangement of hydrogen-bond network around Lys102, overview
-
-
?
Orotidine 5'-phosphate
UMP + CO2
the enzyme catalyzes the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates, active site residues in ODCase are involved in an extensive hydrogen-bonding network, active site Lys42
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
absolutely specific
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
absolutely specific
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic mechanism involving protonation at O2 and a proposed Zn2+ interaction at O4, role of Lys-93 in catalysis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic proficiency, activity does not depend on the formation of a covalent bond to the substrate, catalyzes the reaction through noncovalent binding interactions that involve only the functional groups of its constituent amino acids, catalytic mechanism, mechanism of transition state stabilization, active site structure, role of Lys-93
-
ir
Orotidine 5'-phosphate
UMP + CO2
-
enzyme has two functionally independent substrate binding sites
-
?
Orotidine 5'-phosphate
UMP + CO2
enzyme/active site structure, mode of substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, carbanion intermediate is stabilized by simple electrostatic interaction with Lys-93, the driving force of reaction is ground state destabilization resulting from charge repulsion between the carboxyl of the substrate and Asp-91
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the integrity of the network of the charged residues within the active site, Lys-59, Asp-91, Lys-93 and Asp-96, is essential for transition state stabilization, altered substrate is very tightly bound in the transition state, mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the critical final step in the pyrimidine biosynthetic pathway
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
catalyzes the final step of pyrimidine biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the enzyme is the most effective pure protein catalyst known in nature
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
act upon its substrate without the intervention of metals or other cofactors and without the formation of covalent bonds between the enzyme and the substrate, substrate binding forces the substrates scissile carboxylate group into the neighborhood of several charged groups at the active site, reaction mechanism, overview
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the decarboxylase shows an extremely fast rate acceleration, 1017-fold rate enhancement, ODCase associates weakly with the substrate in the ground state, but then tightens its grip as the altered substrate approaches the chemical transition state, yielding a complex with an estimated dissociation constant Ktx of over 10-24 M
-
-
?
Orotidine 5'-phosphate
UMP + CO2
stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic mechanism involving protonation at O2 and a proposed Zn2+ interaction at O4, role of Lys-93 in catalysis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the enzyme is required for de novo pyrimidine synthesis catalyzing the key final step in de novo synthesis of UMP
-
-
?
orotidine 5'-phosphate + H+
UMP + CO2
-
-
-
-
?
orotidine 5'-phosphate + H+
UMP + CO2
-
-
-
-
?
additional information
?
-
theoretical studies of the effect of thio substitution on orotidine monophosphate decarboxylase substrates
-
-
?
additional information
?
-
Methanobacterium thermoautotrophicus
computed kinetic isotope effects support a direct decarboxylation mechanism. Data suggest a role for Lys72 in stabilizing the transition state in the catalysis of orotidine 5'-phosphate and, to a somewhat lesser extent, in 5-fluoro-orotidine 5'-phosphate
-
-
?
additional information
?
-
Methanobacterium thermoautotrophicus DSM 1053
computed kinetic isotope effects support a direct decarboxylation mechanism. Data suggest a role for Lys72 in stabilizing the transition state in the catalysis of orotidine 5'-phosphate and, to a somewhat lesser extent, in 5-fluoro-orotidine 5'-phosphate
-
-
?
additional information
?
-
-
not: 2-thioorotidine 5'-phosphate
-
?
additional information
?
-
-
the enzyme also converts 6-cyano-UMP to barbituric acid monophosphate with low activity
-
-
?
additional information
?
-
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
?
additional information
?
-
-
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
?
additional information
?
-
-
2-thioorotidine 5'-phosphate is 10000000fold less reactive than orotidine 5'-phosphate as substrate, not: 2-thiouridine 5'-phosphate
-
?
additional information
?
-
-
not: 2-thioorotidine 5-phosphate, undetectable activity with CMP-6-carboxylate and weak binding to ODCase
-
?
additional information
?
-
-
the yeast enzyme does not exhibit a measurable affinity for a substrate analogue in which the labile carboxylate group is replaced by a cationic substituent, the apo and ligand-bound forms of the enzyme show distinct open and closed forms, the closed form is catalytically competent
-
-
?
additional information
?
-
-
in reaction model phosphodianion binding interactions are utilized to stabilize a rare closed enzyme form that exhibits a high catalytic activity for decarboxylation. The thermodynamic barrier to formation of the productive catalytic complex from the inactive enzyme arises largely from the desolvation of the active site accompanying the conformational change and sequestration of the substrate from bulk solvent. The energetically unfavorable conformational change and desolvation of the active site are paid for by the binding energy available from the formation of strong phosphodianion-protein interactions in the desolvated environment present at the EC·S complex. The phosphodianion binding energy is recovered as transition state stabilization via the enhanced electrostatic and hydrogen bonding interactions at the transition state in the desolvated active site
-
-
?
additional information
?
-
-
the total transition-state stabilization for decarboxylation of orotidine 5'-phosphate via the UMP vinyl carbanion intermediate exceeds that for the formation of this carbanion by proton transfer from C-6 of UMP to the enzyme by ca.17 kcal/mol. A large portion of the total transition-state stabilization for the decarboxylation of orotidine 5'-monophosphate can be accounted for by stabilization of the enzyme-bound vinyl carbanion intermediate of the stepwise reaction
-
-
?
additional information
?
-
extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview
-
-
?
additional information
?
-
ScOMPDC also catalyzes decarboxylation of 1-(beta-D-erythrofuranosyl)-5-fluoroorotate (FEO), of 5-fluoroorotate (FO), and of 1-(beta-D-erythrofuranosyl)-orotic acid (EO). Open and the closed forms of enzyme ScOMPDC: phosphodianion gripper loop (with structural heterogeneity between organisms) and pyrimidine umbrella, structure, overview. Reaction mechanism and kinetics with different substrates, transition state analysis
-
-
?
additional information
?
-
two flexible loops close to form the active site cage: Pro202-Val220, on the left-hand side of each structure, interact with the substrate dianion, and Glu152-Thr165, on the right-hand side, interact with the pyrimidine ring. The tyrosyl phenol group stabilizes the closed form of ScOMPDC by hydrogen bonding to the substrate phosphodianion, and that the phenyl group of Y217 and F217 facilitates formation of the transition state for the rate-limiting conformational change
-
-
?
additional information
?
-
ScOMPDC also catalyzes decarboxylation of 1-(beta-D-erythrofuranosyl)-5-fluoroorotate (FEO), of 5-fluoroorotate (FO), and of 1-(beta-D-erythrofuranosyl)-orotic acid (EO). Open and the closed forms of enzyme ScOMPDC: phosphodianion gripper loop (with structural heterogeneity between organisms) and pyrimidine umbrella, structure, overview. Reaction mechanism and kinetics with different substrates, transition state analysis
-
-
?
additional information
?
-
two flexible loops close to form the active site cage: Pro202-Val220, on the left-hand side of each structure, interact with the substrate dianion, and Glu152-Thr165, on the right-hand side, interact with the pyrimidine ring. The tyrosyl phenol group stabilizes the closed form of ScOMPDC by hydrogen bonding to the substrate phosphodianion, and that the phenyl group of Y217 and F217 facilitates formation of the transition state for the rate-limiting conformational change
-
-
?
additional information
?
-
extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview
-
-
?
additional information
?
-
-
not: 2-thioorotidine 5-phosphate, undetectable activity with CMP-6-carboxylate and weak binding to ODCase
-
?
additional information
?
-
-
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
1-methylorotate
-
modeling of binding and structure
1-Ribosyloxipurinol 5'-phosphate
2'-deoxy-2'-fluoro-6-iodo-beta-D-uridine 5'-O-monophosphate
2'-deoxy-2'-fluoro-6-iodo-UMP
2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl-cytosine
2'-deoxyuridine 5'-phosphate
competitive inhibition, at higher concentrations
2- thiouridine 5'-phosphate
-
mixed inhibition
3-Xanthosine 5'-phosphate
-
-
4-(2-hydroxy-4-methoxyphenyl)-4-oxobutanoic acid
the inhibitor molecule occupies a part of the active site that overlaps with the phosphate-binding region in the OMP- or UMP-bound complexes. The carboxyl group of the inhibitor causes a dramatic movement of the L1 and L2 loops that play a role in the recognition of the substrate and product molecules
4-thiouridine 5'-phosphate
-
competitive inhibition, stronger inhibitor than UMP
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,6-dihydro-6-sulfonyl-OMP
-
inhibitor with high affinity for the enzyme
5,6-dihydro-6-sulfonyl-UMP
-
inhibitor with high affinity for the enzyme
5,6-dihydroorotidine 5'-phosphate
-
-
5-(2-(N-(2-Acetamidoethyl)carbamyl)ethyl)-6-azauridine 5'phosphate
-
maximal inhibition at pH 8.3
5-(2-(N-(2-Aminoethyl)carbamyl)ethyl)-6-azauridine 5'-phosphate
-
-
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
5-fluorouracil
-
1 mM, 14% inhibition
5-phosphoribofuranosylallopurinol
-
-
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
6-amino-1-methyluracil
-
modeling of binding and structure
6-amino-UMP
-
competitive inhibition
6-amino-uridine 5'-monophosphate
-
6-aminouridine 5'-monophosphate
6-aminouridine 5'-phosphate
-
-
6-aza-uridine 5'-monophosphate
-
6-Azauracil
-
competitive inhibitor
6-azauridine 5'-monophosphate
6-azauridine 5'-phosphate
6-azido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
6-azido-uridine 5'-monophosphate
-
6-azidouridine 5'-monophosphate
6-azidouridine 5'-phosphate
-
-
6-carboxyamidouridine 5'-phosphate
-
-
6-cyano-1-methyluracil
-
modeling of binding and structure
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
6-cyano-UMP
-
competitive inhibition
6-cyano-uridine 5'-monophosphate
-
6-cyanouridine 5'-monophosphate
6-cyanouridine 5'-phosphate
6-hydroxy UMP
-
inhibits activity with orotidine and orotidine 5'-phosphate, mutant enzyme C155S
6-hydroxy-1-methyl uracil
-
modeling of binding and structure
6-hydroxyUMP
-
a transition state analogue inhibitor, binding structure in complex with the enzyme, overview
6-hydroxyuridine 5'-monophosphate
6-hydroxyuridine 5'-phosphate
6-iodouridine 5'-monophosphate
6-methyl-uridine 5'-monophosphate
-
6-methyluridine 5'-phosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
6-thiocarboxamidouridine 5'-phosphate
7-Ribosyloxipurinol 5'-phosphate
-
-
8-azaxanthosine 5'-phosphate
-
-
allopurinol beta-D-riboside 5'-phosphate
-
-
allopurinol-3-riboside 5'-monophosphate
-
barbiturate ribonucleoside 5'-monophosphate
Barbituric acid
-
mutant enzyme C155S
barbituric acid monophosphate
-
i.e. 6-hydroxy-UMP
barbituric acid ribonucleoside 5'-monophosphate
beta-D-ribofuranosylbarbiturate 5'-monophosphate
-
potent inhibitor
Dimethylsulfoxide
-
20% v/v, 8% inhibition
EDTA
-
10 mM, 6% inhibition; 10 mM, at 70°C, weak inhibition
guanidine hydrochloride
-
2 M, denaturates
Guanidine-HCl
-
2.0 M, complete inhibition
Guanidinium chloride
-
1 M, at 70°C, 81.4% inhibition
Orotidine
-
mutant enzyme C155S
oxipurinol nucleotides
-
potent, competitive, bimodal. The inhibition of the enzyme by oxipurinol nucleotides is primarily responsible for the increased urinary excretion of orotic acid and orotidine in patients treated with allopurinol
oxypurinol 5'-phosphate
-
-
poly(ADP-D-ribose)n-1
-
-
pyrazofurin 5'-monophosphate
pyrazofurin-5'-monophosphate
SDS
-
1%, at 70°C, complete inactivation; 1%, complete inhibition
thiopurinol 5'-phosphate
-
-
Uracil
-
strong feedback inhibition
xanthosine 5'-monophosphate
(5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate
i.e. CMP-N3-oxide
(5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate
i.e. CMP-N3-oxide
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
mode of binding
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
-
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
reversible
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
-
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
high affinity inhibitor
1-Ribosyloxipurinol 5'-phosphate
-
most effective oxipurinol nucleotide inhibitor
1-Ribosyloxipurinol 5'-phosphate
-
-
2'-deoxy-2'-fluoro-6-iodo-beta-D-uridine 5'-O-monophosphate
-
-
2'-deoxy-2'-fluoro-6-iodo-beta-D-uridine 5'-O-monophosphate
-
-
2'-deoxy-2'-fluoro-6-iodo-UMP
-
-
2'-deoxy-2'-fluoro-6-iodo-UMP
-
-
2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl-cytosine
-
-
2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl-cytosine
-
-
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
5-cyano-UMP
-
poor inhibition
5-cyano-UMP
-
poor inhibition
5-cyano-UMP
-
poor inhibition
5-cyano-UMP
-
poor inhibition
5-cyano-UMP
-
poor inhibition
5-cyano-UMP
-
poor inhibition
5-fluoro-UMP
-
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
poor inhibitor
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
poor inhibitor
6-amino-5-fluorouridine
-
competitive inhibition at submicromolar concentrations
6-amino-5-fluorouridine
-
competitive inhibition at submicromolar concentrations
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
6-aminouridine 5'-monophosphate
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aza-UMP
-
-
6-aza-UMP
-
competitive inhibition
6-aza-UMP
competitive inhibition
6-azauridine
-
potent inhibitor
6-azauridine
-
potent inhibitor
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
6-azauridine 5'-monophosphate
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-phosphate
-
-
6-azauridine 5'-phosphate
-
-
6-azauridine 5'-phosphate
-
mode of binding
6-azauridine 5'-phosphate
-
-
6-azauridine 5'-phosphate
-
-
6-azauridine 5'-phosphate
-
-
6-azauridine 5'-phosphate
-
competitive inhibitor
6-azauridine 5'-phosphate
competitive inhibition
6-azauridine 5'-phosphate
-
-
6-azido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
6-azido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
6-azido-5-fluorouridine
-
irreversible inhibitor
6-azido-5-fluorouridine
-
irreversible inhibitor
6-azido-UMP
-
-
6-azidouridine 5'-monophosphate
-
-
6-azidouridine 5'-monophosphate
-
6-azidouridine 5'-monophosphate
-
-
6-azidouridine 5'-monophosphate
-
-
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
reversible inhibitor
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
reversible inhibitor
6-cyanouridine
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
6-cyanouridine 5'-monophosphate
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-phosphate
-
-
6-cyanouridine 5'-phosphate
-
competitive
6-hydroxyuridine
-
potent inhibitor
6-hydroxyuridine
-
potent inhibitor
6-hydroxyuridine 5'-monophosphate
-
tightly binding competitive inhibitor
6-hydroxyuridine 5'-monophosphate
strong binding of 6-hydroxyuridine 5'-monophosphate (BMP) to OMPDC induces a protein conformational change. This includes closure of the phosphodianion gripper loop (Pro202-Val220) and pyrimidine umbrella (Glu152-Thr165) over the inhibitor, which locks BMP in a protein cage. Interactions of the ligand phosphodianion with the amide side chain of Gln215, the phenol side chain of Tyr217, the guanidine side chain of Arg235, which sits on the protein surface adjacent to the gripper loop and functions cooperatively with the loop side chains in activating OMPDC for catalysis, and with backbone amides from Gly234 and Arg235
6-hydroxyuridine 5'-phosphate
-
potent competitive inhibitor
6-hydroxyuridine 5'-phosphate
mode of binding
6-hydroxyuridine 5'-phosphate
-
-
6-iodouridine
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
6-iodouridine 5'-monophosphate
-
i.e. 6-iodo-UMP, irreversible inhibition, mass spectral analysis of the enzyme-inhibitor complex, binding to the enzyme is accompanied by loss of two protons and the iodo moiety, covalent bond formation
6-iodouridine 5'-monophosphate
-
6-iodouridine 5'-monophosphate
-
irreversible inhibitor
6-iodouridine 5'-monophosphate
i.e. 6-iodo-UMP, irreversible inhibition, mass spectral analysis of the enzyme-inhibitor complex, binding to the enzyme is accompanied by loss of two protons and the iodo moiety, covalent bond formation, the inhibitor exhibits potent antiplasmodial activity
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine
-
potent inhibitor
6-thiocarboxamidouridine
-
potent inhibitor
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-phosphate
-
-
6-thiocarboxamidouridine 5'-phosphate
-
competitive, very strong, reversible inhibition
AMP
-
-
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
barbituric acid ribonucleoside 5'-monophosphate
-
-
barbituric acid ribonucleoside 5'-monophosphate
-
-
barbituric acid ribonucleoside 5'-monophosphate
-
-
barbituric acid ribonucleoside 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
barbituric acid ribonucleoside 5'-monophosphate
-
-
barbituric acid ribonucleoside 5'-monophosphate
-
-
barbituric acid ribonucleoside 5'-monophosphate
-
-
clevudine
-
-
CMP
-
-
dAMP
-
-
gemcitabine
-
-
GMP
-
IMP
-
-
nifedipine
-
competitive inhibition
nifedipine
-
competitive inhibition
nifedipine
-
competitive inhibitor
nifedipine
-
competitive inhibition
nifedipine
-
competitive inhibitor
nifedipine
-
competitive inhibition
nifedipine
-
competitive inhibition
nifedipine
-
competitive inhibition
nimodipine
-
competitive inhibition
nimodipine
-
competitive inhibition
nimodipine
-
competitive inhibitor
nimodipine
-
competitive inhibition
nimodipine
-
competitive inhibitor
nimodipine
-
competitive inhibition
nimodipine
-
competitive inhibition
nimodipine
-
competitive inhibition
phosphate
-
weak
phosphate
-
competitive, mutant enzyme C155S
phosphate
-
low activity in phosphate buffers, inhibitory or destabilizing effect
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin
-
potent inhibitor
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin
-
potent inhibitor
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
pyrazofurin 5'-monophosphate
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
ribose 5-phosphate
-
competitive inhibitor
TMP
-
-
UMP
-
weak inhibitor
UMP
competitive inhibition
UMP
-
ineffective inhibitor
UMP
competitive inhibition
UMP
-
competitive inhibition
UMP
-
1 mM, 19% inhibition; 1 mM, at 70°C, 19% inhibition
Xanthosine
-
potent inhibitor
Xanthosine
-
potent inhibitor
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
Methanococcus thermoautotrophicum
-
-
xanthosine 5'-monophosphate
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-phosphate
-
-
xanthosine 5'-phosphate
competitive inhibition
xanthosine 5'-phosphate
-
-
XMP
-
-
additional information
-
inhibitor synthesis, overview
-
additional information
-
not inhibited by 2-thioorotidine 5'-phosphate
-
additional information
-
not inhibited by zinc-chelating agents, e.g. EDTA
-
additional information
-
not inhibited by 6-carboxamidouridine 5-phosphate, recombinant ODCase expressed in Escherichia coli is not inhibited by 1,3-dimercaptopropanol and EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0052 - 0.01
2'-deoxyorotidine 5'-phosphate
0.02
4-Thioorotidine 5'-phosphate
-
-
0.03
5-Azaorotidine 5'-phosphate
-
-
0.0008 - 0.92
5-Fluoroorotidine 5'-phosphate
0.0007
Orotidine
-
pH 7.2, 23°C, mutant enzyme C155S
0.0016 - 0.13
orotidine 5'-monophosphate
0.0002 - 30
orotidine 5'-phosphate
additional information
additional information
-
0.0052
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, T100A mutant
0.0054
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, wild-type enzyme
0.008
2'-deoxyorotidine 5'-phosphate
-
wild-type enzyme
0.01
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, D37A mutant
0.0008
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C
0.008
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
0.0082
5-Fluoroorotidine 5'-phosphate
-
wild type enzyme
0.055
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A
0.056
5-Fluoroorotidine 5'-phosphate
-
-
0.058
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C
0.086
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A/Q215A
0.096
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
0.41
5-Fluoroorotidine 5'-phosphate
-
K59A mutant
0.42
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
0.58
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
0.62
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217A
0.65
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
0.92
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
0.0016
orotidine 5'-monophosphate
wild type enzyme
0.05
orotidine 5'-monophosphate
Q215A mutant
0.11
orotidine 5'-monophosphate
S154/Q215A mutant
0.13
orotidine 5'-monophosphate
S154 mutant
0.0002
orotidine 5'-phosphate
-
mutant T80S, pH 7.2, 25°C
0.00026
orotidine 5'-phosphate
-
orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase, 20°C
0.000295
orotidine 5'-phosphate
-
orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase
0.00035
orotidine 5'-phosphate
-
0.0006
orotidine 5'-phosphate
-
tetrameric enzyme form
0.0006
orotidine 5'-phosphate
-
22-25°C, pH 7.2, recombinant ODCase expressed in Escherichia coli
0.000615
orotidine 5'-phosphate
-
orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase, 37°C
0.0007
orotidine 5'-phosphate
-
-
0.0007
orotidine 5'-phosphate
-
wild-type enzyme
0.0007
orotidine 5'-phosphate
-
pH 6, 25°C
0.0007
orotidine 5'-phosphate
-
pH 7, 25°C
0.0007
orotidine 5'-phosphate
-
22°C, native ODCase expressed in yeast
0.0007
orotidine 5'-phosphate
pH 7.2, 25°C, wild-type enzyme
0.001
orotidine 5'-phosphate
-
pH 7, increases to either side of pH 7
0.001
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96S, pH 7.1, 25°C
0.001 - 0.002
orotidine 5'-phosphate
-
Km value is very dependent on the NaCl concentration, NaCl increases the Km value
0.0012
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25°C
0.0013
orotidine 5'-phosphate
-
0.0014
orotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
0.0014
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C
0.0015
orotidine 5'-phosphate
-
-
0.0016
orotidine 5'-phosphate
-
solubilized enzyme
0.0016
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
wild-type, pH 7.1, 25°C
0.0017
orotidine 5'-phosphate
-
-
0.0017
orotidine 5'-phosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22°C
0.0018
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
0.002
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OMPDC activity
0.0023
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96T, pH 7.1, 25°C
0.0028
orotidine 5'-phosphate
-
wild-type, pH 7.2, 25°C
0.003
orotidine 5'-phosphate
-
dimeric enzyme form
0.003
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123S, pH 7.1, 25°C
0.0032
orotidine 5'-phosphate
-
pH 8.0, 37°C
0.0032
orotidine 5'-phosphate
multienzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
0.0032
orotidine 5'-phosphate
-
mutant D22G, pH 7.2, 25°C
0.0035
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123N, pH 7.1, 25°C
0.0037
orotidine 5'-phosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22°C
0.0041
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25°C
0.0042
orotidine 5'-phosphate
pH 7.2, 25°C, D37A mutant
0.0046
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155D, pH 7.1, 25°C
0.0047
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155S, pH 7.1, 25°C
0.0048
orotidine 5'-phosphate
-
0.005
orotidine 5'-phosphate
-
-
0.005
orotidine 5'-phosphate
-
pH 7.5, 55°C
0.005
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25°C
0.0053
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25°C
0.0055
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
0.006
orotidine 5'-phosphate
-
-
0.006
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant D70N, pH 7.1, 25°C
0.0067
orotidine 5'-phosphate
pH 7.2, 25°C, T100A mutant
0.0075
orotidine 5'-phosphate
-
membrane-bound enzyme
0.008 - 0.009
orotidine 5'-phosphate
-
-
0.00991
orotidine 5'-phosphate
-
-
0.0105
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OMPDC activity
0.0134
orotidine 5'-phosphate
monofunctional enzyme expressed in Escherichia coli
0.0134
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OMPDC activity
0.0166
orotidine 5'-phosphate
-
0.024
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
0.025
orotidine 5'-phosphate
-
monomeric enzyme form
0.025
orotidine 5'-phosphate
-
Q215A mutant
0.03
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
0.033
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
0.036
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25°C
0.092
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
0.1
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
0.1 - 1
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
0.11
orotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
0.11
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
0.13
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
0.29 - 1.4
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
0.3
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
0.35 - 1.4
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
0.6
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
0.64
orotidine 5'-phosphate
-
K59A mutant
0.7
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
0.73
orotidine 5'-phosphate
-
K59A mutant
0.98
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.4
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C
1.9
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
2.2 - 12.9
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y217F/R235A
6.1 - 27.1
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F/R235A
30
orotidine 5'-phosphate
-
value is higher than 30 mM, pH 7.2, 23°C, mutant enzyme C155S
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic data and mechanism
-
additional information
additional information
-
kinetic properties, catalytic proficiency/efficiency
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics, most proficient enzyme known
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetic analysis of wild-type and mutant enzymes with substrate orotidine 5'-phosphate
-
additional information
additional information
kinetic analysis of wild-type and mutant enzymes with substrates orotidine 5'-phosphate and 5-fluoroorotidine 5'-phosphate, rate and equilibrium constants for the conformational change that traps 5-fluoroorotidine 5'-phosphate at the enzyme active site
-
additional information
additional information
substrate specificity and kinetic analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0017 - 0.16
2'-deoxyorotidine 5'-phosphate
9
4-Thioorotidine 5'-phosphate
-
-
5
5-Azaorotidine 5'-phosphate
-
-
4.7 - 570
5-Fluoroorotidine 5'-phosphate
22
Orotidine
-
pH 7.2, 23°C, mutant enzyme C155S
0.042 - 21
orotidine 5'-monophosphate
0.000007 - 985.8
orotidine 5'-phosphate
additional information
additional information
-
0.0017
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, D37A mutant
0.15
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, wild-type enzyme
0.16
2'-deoxyorotidine 5'-phosphate
pH 7.2, 25°C, T100A mutant
4.7
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
6.6
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A/Q215A
8.2
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217A
16
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A
29
5-Fluoroorotidine 5'-phosphate
-
K59A mutant
49
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
92
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C, presence of 0.1 M NaCl
92
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
95
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C, presence of 0.1 M NaCl
95
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
190
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
242
5-Fluoroorotidine 5'-phosphate
-
wild type enzyme
430
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
570
5-Fluoroorotidine 5'-phosphate
-
-
0.042
orotidine 5'-monophosphate
S154/Q215A mutant
0.082
orotidine 5'-monophosphate
S154 mutant
15
orotidine 5'-monophosphate
wild type enzyme
21
orotidine 5'-monophosphate
Q215A mutant
0.000007
orotidine 5'-phosphate
-
pH 7.2, 23°C, mutant enzyme C155S
0.00023
orotidine 5'-phosphate
-
below, D96A mutant
0.00048
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y217F/R235A
0.0005
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155D, pH 7.1, 25°C
0.01 - 1
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96S, pH 7.1, 25°C
0.01 - 1
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155S, pH 7.1, 25°C
0.024
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant D70N, pH 7.1, 25°C
0.11
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F/R235A
0.19 - 0.2
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
0.24
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
0.34
orotidine 5'-phosphate
-
K59A mutant
0.36
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123S, pH 7.1, 25°C
0.5
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25°C
0.52
orotidine 5'-phosphate
-
K59A mutant
0.56
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
0.64
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123N, pH 7.1, 25°C
0.69
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96T, pH 7.1, 25°C
0.7
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25°C
0.75
orotidine 5'-phosphate
-
0.9
orotidine 5'-phosphate
pH 7.2, 25°C, D37A mutant
1
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
1
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C, presence of 0.1 M NCl
1
orotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
1.1
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
1.1
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
1.4
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
1.5
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.5
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
2 - 8
orotidine 5'-phosphate
-
pH 7, constant above pH 7, declines below pH 7
2
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
2.3
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
3
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
3.2
orotidine 5'-phosphate
-
mutant T80S, pH 7.2, 25°C
4
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
wild-type, pH 7.1, 25°C
4.1
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
4.85
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
5.3
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
6.7
orotidine 5'-phosphate
-
7.2
orotidine 5'-phosphate
pH 7.2, 25°C, T100A mutant
7.5
orotidine 5'-phosphate
monofunctional enzyme expressed in Escherichia coli
7.5
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OMPDC activity
8.1
orotidine 5'-phosphate
-
-
13
orotidine 5'-phosphate
-
22°C, native ODCase expressed in yeast
13.7
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25°C
14 - 20
orotidine 5'-phosphate
-
pH 7.2, 25°C, not affected by NaCl concentration
14.4
orotidine 5'-phosphate
-
mutant D22G, pH 7.2, 25°C
15
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C, presence of 0.1 M NaCl
15
orotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
15.6
orotidine 5'-phosphate
-
pH 8.0, 37°C
19
orotidine 5'-phosphate
-
-
19
orotidine 5'-phosphate
-
22-25°C, pH 7.2, recombinant ODCase expressed in Escherichia coli
20
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
20.7
orotidine 5'-phosphate
-
21
orotidine 5'-phosphate
-
pH 7.5, 55°C
22
orotidine 5'-phosphate
-
wild type enzyme
24
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
24.6
orotidine 5'-phosphate
multienzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
27
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25°C
29.7
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25°C
30.7
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OMPDC activity
41
orotidine 5'-phosphate
-
Q215A mutant
42
orotidine 5'-phosphate
-
wild-type, pH 7.2, 25°C
44
orotidine 5'-phosphate
-
wild-type enzyme
44
orotidine 5'-phosphate
pH 7.2, 25°C, wild-type enzyme
985.8
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OMPDC activity
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
50% reduced kcat-value for 4-thioorotidine 5'-phosphate compared with orotidine 5'-phosphate as substrate
-
additional information
additional information
-
high catalytic proficiency
-
additional information
additional information
-
highly proficient enzyme
-
additional information
additional information
-
remarkable catalytic power
-
additional information
additional information
-
very high catalytic proficiency
-
additional information
additional information
-
very proficient enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00002
1-(beta-D-erythrofuranosyl)-orotate
pH 7.0, 25°C, wild-type enzyme
3 - 26
1-(beta-D-erythrofuranosyl)orotic acid
0.00014
5-Fluoroorotate
pH 7.0, 25°C, wild-type enzyme
0.028 - 12000
5-Fluoroorotidine 5'-phosphate
0.0000003
Orotate
pH 7.0, 25°C, wild-type enzyme
0.000037 - 492900
orotidine 5'-phosphate
3
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/Y217F/R235A, pH 7.1, 25°C
4.2
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/R235A, pH 7.1, 25°C
4.6
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/Y217F, pH 7.1, 25°C
10
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Y217F/R235A, pH 7.1, 25°C
11
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A, pH 7.1, 25°C
12
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Y217F, pH 7.1, 25°C
26
1-(beta-D-erythrofuranosyl)orotic acid
-
wild-type, pH 7.1, 25°C
26
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant R235A, pH 7.1, 25°C
0.028
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y217F/R235A
0.82
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F/R235A
7.23
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
13.2
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217A
53.3
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
76.7
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A/Q215A
158.6
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
160
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C
290.9
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant S154A
1023.9
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
1979
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
11875
5-Fluoroorotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
12000
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C
0.000037 - 0.00022
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y217F/R235A
0.00004
orotidine 5'-phosphate
-
mutant Q215A/Y217F/R235A, pH 7.1, 25°C
0.0001
orotidine 5'-phosphate
pH 7.0, 25°C, wild-type enzyme
0.0041
orotidine 5'-phosphate
-
mutant Y217F/R235A, pH 7.1, 25°C
0.0041 - 0.018
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F/R235A
0.013
orotidine 5'-phosphate
-
mutant Q215A/R235A, pH 7.1, 25°C
0.014 - 0.054
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/R235A
0.13
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
0.46
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155D, pH 7.1, 25°C
0.61
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C
0.8
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
0.91
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25°C
0.91
orotidine 5'-phosphate
pH 7.1, 25°C, mutant R235A
1.5
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.7
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
2.3
orotidine 5'-phosphate
-
mutant Q215A/Y217F, pH 7.1, 25°C
3.4 - 17
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A/Y271F
3.7
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
4
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant D70N, pH 7.1, 25°C
8.5
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
10
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96S, pH 7.1, 25°C
13
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
14
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25°C
15
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
22
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant V155S, pH 7.1, 25°C
67
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
70
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
120
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123S, pH 7.1, 25°C
130
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
170
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25°C
180
orotidine 5'-phosphate
-
mutant Y217F, pH 7.1, 25°C
180
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Y217F
190
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant L123N, pH 7.1, 25°C
260
orotidine 5'-phosphate
-
mutant Q215A, pH 7.1, 25°C
260
orotidine 5'-phosphate
pH 7.1, 25°C, mutant Q215A
300
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
mutant I96T, pH 7.1, 25°C
559.7
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OMPDC activity
750
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
2000
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
wild-type, pH 7.1, 25°C
2900
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
2923.8
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OMPDC activity
4500
orotidine 5'-phosphate
-
mutant D22G, pH 7.2, 25°C
5100
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25°C
5900
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25°C
11000
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25°C
11000
orotidine 5'-phosphate
pH 7.1, 25°C, wild-type enzyme
12000
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25°C
15000
orotidine 5'-phosphate
-
mutant T80S, pH 7.2, 25°C
15000
orotidine 5'-phosphate
-
wild-type, pH 7.2, 25°C
492900
orotidine 5'-phosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OMPDC activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D22G
-
30% of wild-type activity
D71C
-
0.9% of wild-type activity
D76C
-
1.1% of wild-type activity
L130M
-
34% of wild-type activity
Q201H
-
80% of wild-type activity
T80S
-
100% of wild-type activity
V167N
-
39% of wild-type activity
D70N
Methanobacterium thermoautotrophicus
0.002% of wild-type activity
D70N/I96S
Methanobacterium thermoautotrophicus
complete loss of activity
D70N/L123S
Methanobacterium thermoautotrophicus
complete loss of activity
D70N/V155S
Methanobacterium thermoautotrophicus
complete loss of activity
I96S
Methanobacterium thermoautotrophicus
0.5% of wild-type activity
I96T
Methanobacterium thermoautotrophicus
15% of wild-type activity
L123N
Methanobacterium thermoautotrophicus
10% of wild-type activity
L123S
Methanobacterium thermoautotrophicus
8% of wild-type activity
V155D
Methanobacterium thermoautotrophicus
less than 0.001% of wild-type activity
V155S
Methanobacterium thermoautotrophicus
1% of wild-type activity
D70N
Methanobacterium thermoautotrophicus DSM 1053
-
0.002% of wild-type activity
-
I96S
Methanobacterium thermoautotrophicus DSM 1053
-
0.5% of wild-type activity
-
I96T
Methanobacterium thermoautotrophicus DSM 1053
-
15% of wild-type activity
-
L123N
Methanobacterium thermoautotrophicus DSM 1053
-
10% of wild-type activity
-
D70A/K72A
-
active site double mutant, markedly less stable than native enzyme
D70G
-
active site mutant, markedly less stable than native enzyme
D70N
-
active site mutant
D75N
-
mutation of an active site residue contributed by the other monomer in the active dimer
K42A
-
active site mutant
K72A
-
inactive active site mutant
K82A
crystallization data
Q185A/R203A
loss of activity
R160A
43fold decrease in catalytic efficiency
R160A/R203A
loss of activity
R160A/V182A
1700fold decrease in catalytic efficiency
R203A
1900fold decrease in catalytic efficiency
R203A/R160A
crystallization data
R203A/T159V
crystallization data
R203A/V182A
crystallization data
S127A
-
active site mutant, orotate recognition mutant
T159A
crystallization data
T159S
crystallization data
T159V
41fold decrease in catalytic efficiency
T159V/R203A
loss of activity
T159V/V182A
3600fold decrease in catalytic efficiency
T159V/V182A/Y206F
20000fold decrease in catalytic efficiency
T159V/Y206F
780fold decrease in catalytic efficiency
V182A
22fold decrease in catalytic efficiency
V182A/R203A
loss of activity
V182A/Y206F
190fold decrease in catalytic efficiency
Y206F
4fold decrease in catalytic efficiency
Q185A
-
220fold decrease in catalytic efficiency
-
R160A
-
43fold decrease in catalytic efficiency
-
R203A
-
1900fold decrease in catalytic efficiency
-
T159A
-
crystallization data
-
Y206F
-
4fold decrease in catalytic efficiency
-
K93C
-
K93C has no activity, affinities for the competitive inhibitor 6-azauridylate and UMP are significantly altered from the pattern with the wild type enzyme
D37A
300fold reduced kcat/Km value
D96A/C155S
-
inactive mutant protein
Q215A/S154A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
T100A
60fold reduced kcat/Km value
Y217A
-
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics, the Y217A mutation results in large decreases in kcat/Km for ScOMPDC-catalyzed decarboxylation of both orotidine 5'-phosphate and 5-fluoroorotidine 5'-phosphate, because of the comparable effects of this mutation on rate-determining decarboxylation of enzyme-bound OMP and on the rate-determining enzyme conformational change for decarboxylation of 5-fluoroorotidine 5'-phosphate
-
Y217F
-
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
-
K93C
-
absence of Zn2+ in mutant ODCase
-
D70A
-
active site mutant
D70A
-
inactive active site mutant
Q185A
-
active site mutant, orotate recognition mutant
Q185A
220fold decrease in catalytic efficiency
R160A/Y206F
crystallization data
R160A/Y206F
340fold decrease in catalytic efficiency
C155S
-
mutant
C155S
-
more stable than wild-type enzyme
C155S
-
the mutant is more stable than the wild-type enzyme but retains the catalytic properties of the wild-type enzyme
D91A
-
inactive mutant
D91A
-
inactive mutant, reduced activity by 5 orders of magnitude, no substrate binding
D91A
-
mutant with strongly reduced activity, incapable of binding substrate
D96A
-
active site mutant with increased dissociation constants for various ligands and strongly reduced activity
D96A
-
inactive mutant, reduced kcat-value by more than 5 orders of magnitude, 11fold decrease in the affinity for the substrate in the ground state
K59A
-
mutant
K59A
-
130fold reduced kcat-value, 900fold increased Km-value
K59A
-
active site mutant with increased dissociation constants for various ligands and strongly reduced activity
K93A
-
inactive mutant, reduced activity by 5 orders of magnitude, no substrate binding
K93A
-
mutant with strongly reduced activity, incapable of binding substrate
K93C
-
absence of Zn2+ in mutant ODCase
K93C
-
inactive mutant, rescue of the mutant with bromethylamine restores activity
Q215A
site-directed mutagenesis
Q215A
-
same activity as wild-type enzyme
Q215A
-
2.5% of wild-type activity
Q215A
mutant, effect of the mutation of the kinetic parameters for decarboxylation is determined
Q215A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
Q215A
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
Q215A/R235A
-
less than 0.1% of wild-type activity
Q215A/R235A
site-directed mutagenesis, mutation of residues in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics, the mutation causes a large decrease in the kinetic parameters for ScOMPDC-catalyzed decarboxylation of OMP, which are limited by the rate of the decarboxylation step, but much smaller decreases in the kinetic parameters for ScOMPDC-catalyzed decarboxylation of 5-fluoroorotidine 5'-phosphate, which are limited by the rate of enzyme conformational changes
Q215A/R235A
site-directed mutagenesis, no dianion activation
Q215A/Y217F
-
less than 0.1% of wild-type activity
Q215A/Y217F
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
Q215A/Y217F/R235A
-
effect of the triple mutation on the catalytic activity toward OMP can be ascribed almost entirely to the loss of stabilizing interactions of the three excised side chains with the transition state for decarboxylation
Q215A/Y217F/R235A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
Q215A/Y217F/R235A
site-directed mutagenesis, no dianion activation
Q215A/Y217F/R235A
site-directed mutagenesis, triple mutation results in only a 9fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
R235A
-
active site mutant with increased dissociation constants for various ligands
R235A
-
less than 0.1% of wild-type activity
R235A
-
mutation results in 12000fold decrease in catalytic efficiency with substrate orotidine 5'-phosphate and 75fold decrease with substrate 5-fluoroorotidine 5'-phosphate. The effect of the R235A mutation on the enzyme-catalyzed deuterium exchange is expressed predominantly as a change in the turnover number kex, whereas the effect on the enzyme-catalyzed decarboxylation of orotidine 5'-phosphate is expressed predominantly as a change in the Michaelis constant Km
R235A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
R235A
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
S154A
site-directed mutagenesis
S154A
mutant, effect of the mutation of the kinetic parameters for decarboxylation is determined
S154A
site-directed mutagenesis, the stabilizing interactions between the 5-F and neighboring C-6 carbanion are strongly expressed at the rate-determining transition state for decarboxylation of FOMP catalyzed by S154A mutant ScOMPDC
S154A/Q215A
site-directed mutagenesis
S154A/Q215A
mutant, effect of the mutation of the kinetic parameters for decarboxylation is determined
Y217A
-
active site mutant with increased dissociation constants for various ligands
Y217A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics, the Y217A mutation results in large decreases in kcat/Km for ScOMPDC-catalyzed decarboxylation of both orotidine 5'-phosphate and 5-fluoroorotidine 5'-phosphate, because of the comparable effects of this mutation on rate-determining decarboxylation of enzyme-bound OMP and on the rate-determining enzyme conformational change for decarboxylation of 5-fluoroorotidine 5'-phosphate
Y217F
-
1.6% of wild-type activity
Y217F
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
Y217F
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
Y217F/R235A
-
less than 0.1% of wild-type activity
Y217F/R235A
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
Y217F/R235A
site-directed mutagenesis, no dianion activation
Q215A
-
site-directed mutagenesis
-
Q215A
-
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
-
Q215A
-
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
-
R235A
-
site-directed mutagenesis, the mutation results in an about 2.4fold decrease in kcat/Km for decarboxylation of 1-(beta-D-erythrofuranosyl)-orotic acid
-
R235A
-
site-directed mutagenesis, mutation of a residue in the phosphodianion gripper loop reducing the catalytic efficiency and altering kinetics
-
S154A
-
site-directed mutagenesis
-
S154A
-
site-directed mutagenesis, the stabilizing interactions between the 5-F and neighboring C-6 carbanion are strongly expressed at the rate-determining transition state for decarboxylation of FOMP catalyzed by S154A mutant ScOMPDC
-
additional information
Methanobacterium thermoautotrophicus
substitutions of hydrophobic residues in a pocket proximal to the carboxylate group of the substrate, i.e. Ile 96, Leu 123, and Val 155 with neutral hydrophilic residues decrease the value of kcat by as much as 400fold but have minimal effect on the value of kex for exchange of H6 of the 5-fluoro-UMP product analog with solvent deuterium
additional information
Methanobacterium thermoautotrophicus DSM 1053
-
substitutions of hydrophobic residues in a pocket proximal to the carboxylate group of the substrate, i.e. Ile 96, Leu 123, and Val 155 with neutral hydrophilic residues decrease the value of kcat by as much as 400fold but have minimal effect on the value of kex for exchange of H6 of the 5-fluoro-UMP product analog with solvent deuterium
-
additional information
the orotidine 5'-phosphate decarboxylase encoding gene, pm-ura3, from Pestalotiopsis microspora strain NK17 is utilized as a marker in the construction of a reusable system for gene scarless deletion, restoration, and tagging. As a positive marker, gene pm-ura3 can be used to targeted locus of interest in a start uracil auxotrophic host. It then can be replaced by any artificial DNA sequence, e.g. a mutated ORF, under the negative selection of 5-fluoroorotic acid. By this method, genes of interest can be edited in situ and the marker can be recycled. The system is applied to study the function of pm-mus53, it is observed that the gene has little effect on the nonhomologous end-joining process mediated by Agrobacterium tumefaciens-mediated transformation. The expression of a putative taxadiene synthase in taxol biosynthetic pathways of Pestalotiopsis microspora is investigated revealing that it is differentially expressed in solid and liquid medium. Method overview
additional information
-
the orotidine 5'-phosphate decarboxylase encoding gene, pm-ura3, from Pestalotiopsis microspora strain NK17 is utilized as a marker in the construction of a reusable system for gene scarless deletion, restoration, and tagging. As a positive marker, gene pm-ura3 can be used to targeted locus of interest in a start uracil auxotrophic host. It then can be replaced by any artificial DNA sequence, e.g. a mutated ORF, under the negative selection of 5-fluoroorotic acid. By this method, genes of interest can be edited in situ and the marker can be recycled. The system is applied to study the function of pm-mus53, it is observed that the gene has little effect on the nonhomologous end-joining process mediated by Agrobacterium tumefaciens-mediated transformation. The expression of a putative taxadiene synthase in taxol biosynthetic pathways of Pestalotiopsis microspora is investigated revealing that it is differentially expressed in solid and liquid medium. Method overview
-
additional information
construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
-
construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
structure-function analysis of mutant enzymes, compared to the wild-type, overview
additional information
-
structure-function analysis of mutant enzymes, compared to the wild-type, overview
-
additional information
-
construction of a null mutant, allelic replacement mutagenesis of pyrF, phenotype, overview, unlike the wild-type strain, an isogenic pyrF mutant is resistant to 5-fluoroorotic acid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Murray, M.G.; Ross, C.
Molecular weight estimations of some pyrimidine-metabolizing enzymes from pea cotyledons by gel filtration
Phytochemistry
10
2645-2648
1971
Pisum sativum
-
brenda
Fyfe, J.A.; Miller, R.L.; Krenitsky, T.A.
Kinetic properties and inhibition of orotidine 5'-phosphate decarboxylase. Effects of some allopurinol metabolites on the enzyme
J. Biol. Chem.
248
3801-3809
1973
Saccharomyces cerevisiae
brenda
Shoaf, W.T.; Jones, M.E.
Uridylic acid synthesis in Ehrlich ascites carcinoma. Properties, subcellular distribution, and nature of enzyme complexes of six biosynthetic enzymes
Biochemistry
12
4039-4051
1973
Mus musculus
brenda
Brown, G.K.; Fox, R.M.; O'Sullivan, W.J.
Interconversion of different molecular weight forms of human erythrocyte orotidylate decarboxylase
J. Biol. Chem.
250
7352-7358
1975
Homo sapiens
brenda
Yoshimoto, A.; Umezu, K.; Kobayashi, K.; Tomita, K.
Orotidylate decarboxylase (yeast)
Methods Enzymol.
51
74-79
1978
Saccharomyces cerevisiae
brenda
Brody, R.S.; Westheimer, F.H.
The purification of orotidine-5'-phosphate decarboxylase from yeast by affinity chromatography
J. Biol. Chem.
254
4238-4244
1979
Saccharomyces cerevisiae
brenda
Oakley, B.R.; Rinehart, J.E.; Mitchell, B.L.; Oakley, C.E.; Carmona, C.; Gray, G.L.; May, G.S.
Cloning, mapping and molecular analysis of the pyrG (orotidine-5'-phosphate decarboxylase) gene of Aspergillus nidulans
Gene
61
385-399
1987
Aspergillus nidulans
brenda
Langdon, S.D.; Jones, M.E.
Study of the kinetic and physical properties of the orotidine-5'-monophosphate decarboxylase domain from mouse UMP synthase produced in Saccharomyces cerevisiae
J. Biol. Chem.
262
13359-13365
1987
Mus musculus
brenda
Reiter, S.; Grbner, W.
Orotidine-5'-phosphate decarboxylase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
338-346
1984
Saccharomyces cerevisiae, Mus musculus, Rattus norvegicus
-
brenda
Pragobpol, S.; Gero, A.M.; Lee, C.S.; O'Sullivan, W.J.
Orotate phosphoribosyltransferase and orotidylate decarboxylase from Crithidia luciliae: subcellular location of the enzymes and a study of substrate chanelling
Arch. Biochem. Biophys.
230
285-293
1984
Crithidia luciliae
brenda
Donovan, W.P.; Kushner, S.R.
Purification and characterization of orotidine-5'-phosphate decarboxylase from Escherichia coli K-12
J. Bacteriol.
156
620-624
1983
Escherichia coli
brenda
Levine, H.L.; Brody, R.S.; Westheimer, F.H.
Inhibition of orotidine-5'-phosphate decarboxylase by 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid, 6-azauridine 5'-phosphate and uridine 5'-phosphate
Biochemistry
19
4993-3999
1980
Saccharomyces cerevisiae
brenda
Floyd, E.E.; Jones, M.E.
Isolation and characterization of the orotidine 5'-monophosphate decarboxylase domain of the multifunctional protein uridine 5'-monophosphate synthase
J. Biol. Chem.
260
9443-9451
1985
Mus musculus
brenda
Smiley, J.A.; Paneth, P.; O'Leary, M.H.; Bell, J.B.; Jones, M.E.
Investigation of the enzymatic mechanism of yeast orotidine-5'-monophosphate decarboxylase using 13C kinetic isotope effects
Biochemistry
25
6216-6223
1991
Saccharomyces cerevisiae
brenda
Acheson, S.A.; Bell, J.B.; Jones, M.E.; Wolfenden, R.
Orotidine-5'-monophosphate decarboxylase catalysis: kinetic isotope effects and the state of hybridization of a bound transition-state analogue
Biochemistry
29
3198-3202
1990
Saccharomyces cerevisiae, Saccharomyces cerevisiae 15C
brenda
Smiley, J.A.; Jones, M.E.
A unique catalytic and inhibitor-binding role of Lys93 of yeast orotidylate decarboxylase
Biochemistry
31
12162-12168
1992
Mus musculus
brenda
Miller, B.G.; Traut, T.W.; Wolfenden, R.
A role for zinc in OMP decarboxylase, an unusually proficient enzyme
J. Am. Chem. Soc.
120
2666-2667
1998
Saccharomyces cerevisiae
-
brenda
Shostak, K.; Jones, E.
Orotidylate decarboxylase: insights into the catalytic mechanism from substrate specificity studies
Biochemistry
31
12155-12161
1992
Saccharomyces cerevisiae
brenda
Jones, M.E.
Orotidylate decarboxylase of yeast and man
Curr. Top. Cell. Regul.
33
331-342
1992
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Yablonski, M.J.; Pasek, D.A.; Han, B.D.; Jones, M.E.; Traut, T.W.
Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase
J. Biol. Chem.
271
10704-10708
1996
Homo sapiens
brenda
Bell, J.B.; Jones, M.E.
Purification and characterization of yeast orotidine 5'-monophosphate decarboxylase overexpressed from plasmid PGU2
J. Biol. Chem.
266
12662-12667
1991
Saccharomyces cerevisiae, Saccharomyces cerevisiae 15C
brenda
Strych, U.; Wohlfarth, S.; Winkler, U.K.
Orotidine-5'-monophate decarboxylase from Pseudomonas aeruginosa PAO1: cloning, overexpression, and enzyme characterization
Curr. Microbiol.
29
353-359
1994
Pseudomonas aeruginosa
brenda
Bell, J.B.; Jones, M.E.; Carter, C.W.
Crystallization and yeast orotidine 5'-monophosphate decarboxylase complexed with 1-(5'-phospho-beta-D-ribofuranosyl) barbituric acid
Proteins Struct. Funct. Genet.
9
143-151
1991
Saccharomyces cerevisiae
brenda
Wu, N.; Christendat, D.; Dharamsi, A.; Pai, E.F.
Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase
Acta Crystallogr. Sect. D
56
912-914
2000
Methanothermobacter thermautotrophicus
-
brenda
Miller, B.G.; Wolfenden, R.
Catalytic proficiency: the unusual case of OMP decarboxylase
Annu. Rev. Biochem.
71
847-885
2002
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli
brenda
Smiley, J.A.; DelFraino, B.J.; Simpson, B.A.
Hydrogen isotope tracing in the reaction of orotidine-5'-monophosphate decarboxylase
Arch. Biochem. Biophys.
412
267-271
2003
Saccharomyces cerevisiae
brenda
Cui, W.; DeWitt, J.G.; Miller, S.M.; Wu, W.
No metal cofactor in orotidine 5'-monophosphate decarboxylase
Biochem. Biophys. Res. Commun.
259
133-135
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ5464
brenda
Porter, D.J.T.; Short, S.A.
Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation
Biochemistry
39
11788-11800
2000
Saccharomyces cerevisiae
brenda
Harris, P.; Poulsen, J.C.N.; Jensen, K.F.; Larsen, S.
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase
Biochemistry
39
4217-4224
2000
Escherichia coli
brenda
Rishavy, M.A.; Cleland, W.W.
Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects
Biochemistry
39
4569-4574
2000
Saccharomyces cerevisiae
brenda
Miller, B.G.; Butterfoss, G.L.; Short, S.A.; Wolfenden, R.
Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization?
Biochemistry
40
6227-6232
2001
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae
brenda
Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
41
3861-3869
2002
Bacillus subtilis
brenda
Wu, N.; Gillon, W.; Pai, E.F.
Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography
Biochemistry
41
4002-4011
2002
Methanothermobacter thermautotrophicus
brenda
Smiley, J.A.; Saleh, L.
Active site probes for yeast OMP decarboxylase: inhibition constants of UMP and thio-substituted UMP analogues and greatly reduced activity toward CMP-6-carboxylate
Bioorg. Chem.
27
297-306
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ5424
-
brenda
Gao, J.
Catalysis by enzyme conformational change as illustrated by orotidine 5'-monophosphate decarboxylase
Curr. Opin. Struct. Biol.
13
184-192
2003
Methanothermobacter thermautotrophicus
brenda
Maiorano, J.N.; Grogan, D.W.
Extremely thermostable orotidine-5'-monophosphate decarboxylase from the archaeon Sulfolobus acidocaldarius
FEMS Microbiol. Lett.
174
81-87
1999
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DG6 / ATCC 49426
-
brenda
Quiles-Rosillo, M.D.; Ruiz-Vazquez, R.M.; Torres-Martinez, S.; Garre, V.
Cloning, characterization and heterologous expression of the Blakeslea trispora gene encoding orotidine-5'-monophosphate decarboxylase
FEMS Microbiol. Lett.
222
229-236
2003
Blakeslea trispora (Q870M2), Blakeslea trispora, Blakeslea trispora NRRL2895(+) (Q870M2)
brenda
Lee, T.S.; Chong, L.T.; Chodera, J.D.; Kollman, P.A.
An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase
J. Am. Chem. Soc.
123
12837-12848
2001
Methanothermobacter thermautotrophicus
brenda
Miller, B.G.; Smiley, J.A.; Short, S.A.; Wolfenden, R.
Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals
J. Biol. Chem.
274
23841-23843
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ5424
brenda
Miller, B.G.; Snider, M.J.; Wolfenden, R.; Short, S.A.
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase
J. Biol. Chem.
276
15174-15176
2001
Saccharomyces cerevisiae
brenda
Harris, P.; Poulsen, J.C.N.; Jensen, K.F.; Larsen, S.
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase
J. Mol. Biol.
318
1019-1029
2002
Escherichia coli
brenda
Appleby, T.C.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase
Proc. Natl. Acad. Sci. USA
97
2005-2010
2000
Bacillus subtilis (P25971), Bacillus subtilis
brenda
Wu, N.; Mo, Y.; Gao, J.; Pai, E.F.
Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase
Proc. Natl. Acad. Sci. USA
97
2017-2022
2000
Methanothermobacter thermautotrophicus
brenda
Krungkrai, S.R.; Prapunwattana, P.; Horii, T.; Krungkrai, J.
Orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase exist as multienzyme complex in human malaria parasite Plasmodium falciparum
Biochem. Biophys. Res. Commun.
318
1012-1018
2004
Plasmodium falciparum
brenda
Krungkrai, S.R.; DelFraino, B.J.; Smiley, J.A.; Prapunwattana, P.; Mitamura, T.; Horii, T.; Krungkrai, J.
A novel enzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase in human malaria parasite Plasmodium falciparum: physical association, kinetics, and inhibition characterization
Biochemistry
44
1643-1652
2005
Plasmodium falciparum (Q8T6J6), Plasmodium falciparum
brenda
Sievers, A.; Wolfenden, R.
The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylase
Bioorg. Chem.
33
45-52
2005
Saccharomyces cerevisiae
brenda
Callahan, B.P.; Bell, A.F.; Tonge, P.J.; Wolfenden, R.
A Raman-active competitive inhibitor of OMP decarboxylase
Bioorg. Chem.
34
59-65
2006
Saccharomyces cerevisiae
brenda
Amyes, T.L.; Richard, J.P.; Tait, J.J.
Activation of orotidine 5'-monophosphate decarboxylase by phosphite dianion: the whole substrate is the sum of two parts
J. Am. Chem. Soc.
127
15708-15709
2005
Saccharomyces cerevisiae
brenda
Phillips, L.M.; Lee, J.K.
Theoretical studies of the effect of thio substitution on orotidine monophosphate decarboxylase substrates
J. Org. Chem.
70
1211-1221
2005
Bacillus subtilis (P25971)
brenda
Reinoso, C.; Sorais, F.; Nino-Vega, G.A.; Ferminan, E.; San-Blas, G.; Dominguez, A.
Cloning and functional analysis of the orotidine-5'-phosphate decarboxylase gene (PbrURA3) of the pathogenic fungus Paracoccidioides brasiliensis
Yeast
22
739-743
2005
Paracoccidioides brasiliensis (Q9C131), Paracoccidioides brasiliensis
brenda
Wittmann, J.G.; Rudolph, M.G.
Pseudo-merohedral twinning in monoclinic crystals of human orotidine-5-monophosphate decarboxylase
Acta Crystallogr. Sect. D
63
744-749
2007
Homo sapiens (P11172), Homo sapiens
brenda
Krungkrai, S.R.; Tokuoka, K.; Kusakari, Y.; Inoue, T.; Adachi, H.; Matsumura, H.; Takano, K.; Murakami, S.; Mori, Y.; Kai, Y.; Krungkrai, J.; Horii, T.
Crystallization and preliminary crystallographic analysis of orotidine 5-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum
Acta Crystallogr. Sect. F
F62
542-545
2006
Plasmodium falciparum
brenda
Lewis, C.A.; Wolfenden, R.
Indiscriminate binding by orotidine 5-phosphate decarboxylase of uridine 5-phosphate derivatives with bulky anionic c6 substituents
Biochemistry
46
13331-13343
2007
Saccharomyces cerevisiae
brenda
Callahan, B.P.; Miller, B.G.
OMP decarboxylase - An enigma persists
Bioorg. Chem.
35
465-469
2007
Saccharomyces cerevisiae
brenda
De Maeseneire, S.L.; De Groeve, M.R.; Dauvrin, T.; De Mey, M.; Soetaert, W.; Vandamme, E.J.
Cloning, sequence analysis and heterologous expression of the Myrothecium gramineum orotidine-5-monophosphate decarboxylase gene
FEMS Microbiol. Lett.
261
262-271
2006
Myrothecium gramineum (Q2HZ31), Myrothecium gramineum
brenda
Capone, R.F.; Ning, Y.; Pakulis, N.; Alhazzazi, T.; Fenno, J.C.
Characterization of Treponema denticola pyrF encoding orotidine-5-monophosphate decarboxylase
FEMS Microbiol. Lett.
268
261-267
2007
no activity in Treponema pallidum, Treponema denticola
brenda
Tokuoka, K.; Kusakari, Y.; Krungkrai, S.R.; Matsumura, H.; Krungkrai, J.; Horii, T.; Inoue, T.
Structural basis for the decarboxylation of orotidine 5-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase
J. Biochem.
143
69-78
2008
Plasmodium falciparum
brenda
Poduch, E.; Bello, A.M.; Tang, S.; Fujihashi, M.; Pai, E.F.; Kotra, L.P.
Design of inhibitors of orotidine monophosphate decarboxylase using bioisosteric replacement and determination of inhibition kinetics
J. Med. Chem.
49
4937-4945
2006
Methanothermobacter thermautotrophicus
brenda
Bello, A.M.; Poduch, E.; Fujihashi, M.; Amani, M.; Li, Y.; Crandall, I.; Hui, R.; Lee, P.I.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
A potent, covalent inhibitor of orotidine 5-monophosphate decarboxylase with antimalarial activity
J. Med. Chem.
50
915-921
2007
Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
brenda
Wong, F.M.; Capule, C.C.; Wu, W.
Stability of the 6-carbanion of uracil analogues: mechanistic implications for model reactions of orotidine-5-monophosphate decarboxylase
Org. Lett.
8
6019-6022
2006
Saccharomyces cerevisiae
brenda
Langley, D.B.; Shojaei, M.; Chan, C.; Lok, H.C.; Mackay, J.P.; Traut, T.W.; Guss, J.M.; Christopherson, R.I.
Structure and inhibition of orotidine 5-monophosphate decarboxylase from Plasmodium falciparum
Biochemistry
47
3842-3854
2008
Plasmodium falciparum (Q8T6J6), Plasmodium falciparum
brenda
Barnett, S.A.; Amyes, T.L.; Wood, B.M.; Gerlt, J.A.; Richard, J.P.
Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5-monophosphate decarboxylase: a two-part substrate approach
Biochemistry
47
7785-7787
2008
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae
brenda
Van Vleet, J.L.; Reinhardt, L.A.; Miller, B.G.; Sievers, A.; Wallace Cleland, W.
Carbon isotope effect study on orotidine 5-monophosphate decarboxylase: Support for an anionic intermediate
Biochemistry
47
798-803
2008
Saccharomyces cerevisiae
brenda
Hu, H.; Boone, A.; Yang, W.
Mechanism of OMP decarboxylation in orotidine 5-monophosphate decarboxylase
J. Am. Chem. Soc.
130
14493-14503
2008
Methanothermobacter thermautotrophicus
brenda
Amyes, T.L.; Wood, B.M.; Chan, K.; Gerlt, J.A.; Richard, J.P.
Formation and stability of a vinyl carbanion at the active site of orotidine 5-monophosphate decarboxylase: pKa of the C-6 proton of enzyme-bound UMP
J. Am. Chem. Soc.
130
1574-1575
2008
Saccharomyces cerevisiae
brenda
Poduch, E.; Wei, L.; Pai, E.F.; Kotra, L.P.
Structural diversity and plasticity associated with nucleotides targeting orotidine monophosphate decarboxylase
J. Med. Chem.
51
432-438
2008
Homo sapiens, Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
brenda
Bello, A.M.; Poduch, E.; Liu, Y.; Wei, L.; Crandall, I.; Wang, X.; Dyanand, C.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
Structure-activity relationships of C6-uridine derivatives targeting plasmodia orotidine monophosphate decarboxylase
J. Med. Chem.
51
439-448
2008
Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
brenda
Meza-Avina, M.E.; Wei, L.; Buhendwa, M.G.; Poduch, E.; Bello, A.M.; Pai, E.F.; Kotra, L.P.
Inhibition of orotidine 5-monophosphate decarboxylase and its therapeutic potential
Mini Rev. Med. Chem.
8
239-247
2008
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Plasmodium falciparum, Plasmodium vivax, Methanococcus thermoautotrophicum
brenda
Chien, T.C.; Jen, C.H.; Wu, Y.J.; Liao, C.C.
Chemical models and their mechanistic implications for the transformation of 6-cyanouridine 5-monophosphate catalyzed by orotidine 5-monophosphate decarboxylase
Nucleic Acids Symp. Ser.
52
297-298
2008
Methanothermobacter thermautotrophicus (O26232)
brenda
Kotra, L.P.; Pai, E.F.
Inhibition of orotidine-5-monophosphate decarboxylase--discoveries and lessons
Nucleic Acids Symp. Ser.
52
85-86
2008
Helicobacter pylori, Homo sapiens, Staphylococcus aureus, Plasmodium falciparum, Methanothermobacter thermautotrophicus (O26232)
brenda
Wepukhulu, W.O.; Smiley, V.L.; Vemulapalli, B.; Smiley, J.A.; Phillips, L.M.; Lee, J.K.
A substantial oxygen isotope effect at O2 in the OMP decarboxylase reaction: mechanistic implications
Org. Biomol. Chem.
6
4533-4541
2008
Escherichia coli
brenda
Wittmann, J.G.; Heinrich, D.; Gasow, K.; Frey, A.; Diederichsen, U.; Rudolph, M.G.
Structures of the human orotidine-5-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design
Structure
16
82-92
2008
Homo sapiens (P11172), Homo sapiens
brenda
Yang, F.; Zhang, S.; Tang, W.; Zhao, Z.K.
Identification of the orotidine-5-monophosphate decarboxylase gene of the oleaginous yeast Rhodosporidium toruloides
Yeast
25
623-630
2008
Rhodotorula toruloides (B3GF12), Rhodotorula toruloides
brenda
Meza-Avina, M.E.; Wei, L.; Liu, Y.; Poduch, E.; Bello, A.M.; Mishra, R.K.; Pai, E.F.; Kotra, L.P.
Structural determinants for the inhibitory ligands of orotidine-5'-monophosphate decarboxylase
Bioorg. Med. Chem.
18
4032-4041
2010
Saccharomyces cerevisiae, Helicobacter pylori, Homo sapiens, Methanothermobacter thermautotrophicus, Staphylococcus aureus, Plasmodium falciparum
brenda
Wu, Y.J.; Liao, C.C.; Jen, C.H.; Shih, Y.C.; Chien, T.C.
Chemical models and their mechanistic implications for the transformation of 6-cyanouridine 5-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase
Chem. Commun. (Camb. )
46
4821-4823
2010
Methanothermobacter thermautotrophicus
brenda
Lewis, M.; Meza-Avina, M.E.; Wei, L.; Crandall, I.E.; Bello, A.M.; Poduch, E.; Liu, Y.; Paige, C.J.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
Novel interactions of fluorinated nucleotide derivatives targeting orotidine 5'-monophosphate decarboxylase
J. Med. Chem.
54
2891-2901
2011
Homo sapiens, Methanothermobacter thermautotrophicus
brenda
Huang, S.; Wong, F.M.; Gassner, G.T.; Wu, W.
Accelerated hydrolysis of alpha-halo and alpha-cyano pyridinium relative to uracil derivatives: a model for ODCase-catalyzed hydrolysis of 6-cyanoUMP
Tetrahedron Lett.
52
3960-3962
2011
Homo sapiens
brenda
Iiams, V.; Desai, B.J.; Fedorov, A.A.; Fedorov, E.V.; Almo, S.C.; Gerlt, J.A.
Mechanism of the orotidine 5-monophosphate decarboxylase-catalyzed reaction: importance of residues in the orotate binding site
Biochemistry
50
8497-8507
2011
Methanobacterium thermoautotrophicus (O26232), Methanobacterium thermoautotrophicus DSM 1053 (O26232)
brenda
Amyes, T.L.; Ming, S.A.; Goldman, L.M.; Wood, B.M.; Desai, B.J.; Gerlt, J.A.; Richard, J.P.
Orotidine 5-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions
Biochemistry
51
4630-4632
2012
Saccharomyces cerevisiae
brenda
Desai, B.J.; Wood, B.M.; Fedorov, A.A.; Fedorov, E.V.; Goryanova, B.; Amyes, T.L.; Richard, J.P.; Almo, S.C.; Gerlt, J.A.
Conformational changes in orotidine 5-monophosphate decarboxylase: a structure-based explanation for how the 5-phosphate group activates the enzyme
Biochemistry
51
8665-8678
2012
Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 1053 (O26232)
brenda
Vardi-Kilshtain, A.; Doron, D.; Major, D.T.
Quantum and classical simulations of orotidine monophosphate decarboxylase: support for a direct decarboxylation mechanism
Biochemistry
52
4382-4390
2013
Methanobacterium thermoautotrophicus (O26232), Methanobacterium thermoautotrophicus DSM 1053 (O26232)
brenda
Goryanova, B.; Spong, K.; Amyes, T.L.; Richard, J.P.
Catalysis by orotidine 5-monophosphate decarboxylase: effect of 5-fluoro and 4-substituents on the decarboxylation of two-part substrates
Biochemistry
52
537-546
2013
Saccharomyces cerevisiae
brenda
Goryanova, B.; Goldman, L.M.; Amyes, T.L.; Gerlt, J.A.; Richard, J.P.
Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5-phosphate decarboxylase-catalyzed reactions
Biochemistry
52
7500-7511
2013
Saccharomyces cerevisiae
brenda
Tsang, W.Y.; Wood, B.M.; Wong, F.M.; Wu, W.; Gerlt, J.A.; Amyes, T.L.; Richard, J.P.
Proton transfer from C-6 of uridine 5-monophosphate catalyzed by orotidine 5-monophosphate decarboxylase: formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituent
J. Am. Chem. Soc.
134
14580-14594
2012
Saccharomyces cerevisiae
brenda
Fujihashi, M.; Ishida, T.; Kuroda, S.; Kotra, L.P.; Pai, E.F.; Miki, K.
Substrate distortion contributes to the catalysis of orotidine 5-monophosphate decarboxylase
J. Am. Chem. Soc.
135
17432-17443
2013
Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus DSM 1053 (O26232)
brenda
Takashima, Y.; Mizohata, E.; Krungkrai, S.R.; Fukunishi, Y.; Kinoshita, T.; Sakata, T.; Matsumura, H.; Krungkrai, J.; Horii, T.; Inoue, T.
The in silico screening and X-ray structure analysis of the inhibitor complex of Plasmodium falciparum orotidine 5-monophosphate decarboxylase
J. Biochem.
152
133-138
2012
Plasmodium falciparum (Q8T6J6), Plasmodium falciparum
brenda
Jamshidi, S.; Jalili, S.; Rafii-Tabar, H.
Study of orotidine 5-monophosphate decarboxylase in complex with the top three OMP, BMP, and PMP ligands by molecular dynamics simulation
J. Biomol. Struct. Dyn.
33
404-417
2015
Saccharomyces cerevisiae
brenda
Purohit, M.K.; Poduch, E.; Wei, L.W.; Crandall, I.E.; To, T.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
Novel cytidine-based orotidine-5-monophosphate decarboxylase inhibitors with an unusual twist
J. Med. Chem.
55
9988-9997
2012
Homo sapiens (P11172), Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
brenda
Yuan, J.; Cardenas, A.M.; Gilbert, H.F.; Palzkill, T.
Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase
Protein Sci.
20
1891-1906
2011
Escherichia coli
brenda
Richard, J.P.; Amyes, T.L.; Reyes, A.C.
Orotidine 5'-monophosphate decarboxylase probing the limits of the possible for enzyme catalysis
Acc. Chem. Res.
51
960-969
2018
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae ATCC 204508 / S288c (P03962)
brenda
Imprasittichail, W.; Roytrakul, S.; Krungkrai, S.R.; Krungkrail, J.
A unique insertion of low complexity amino acid sequence underlies protein-protein interaction in human malaria parasite orotate phosphoribosyltransferase and orotidine 5-monophosphate decarboxylase
Asian Pac. J. Trop. Med.
7
184-192
2014
Plasmodium falciparum (A0A1D3TG46), Plasmodium falciparum
brenda
Yaoi, T.; Laksanalamai, P.; Jiemjit, A.; Kagawa, H.; Alton, T.; Trent, J.
Cloning and characterization of ftsZ and pyrF from the archaeon Thermoplasma acidophilum
Biochem. Biophys. Res. Commun.
275
936-945
2000
Thermoplasma acidophilum (O74110), Thermoplasma acidophilum
brenda
Goryanova, B.; Goldman, L.M.; Ming, S.; Amyes, T.L.; Gerlt, J.A.; Richard, J.P.
Rate and equilibrium constants for an enzyme conformational change during catalysis by orotidine 5'-monophosphate decarboxylase
Biochemistry
54
4555-4564
2015
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae ATCC 204508 / S288c (P03962)
brenda
Chen, L.; Wei, D.; Zhang, Q.; Yu, X.; Wang, Y.; Zhu, X.
Orotidine 5'-phosphate decarboxylase-based reusable in situ genetic editing system Development and application in taxol-producing Pestalotiopsis microspora
Eng. Life Sci.
15
542-549
2015
Pestalotiopsis microspora (A0A0A0WDU2), Pestalotiopsis microspora NK17 (A0A0A0WDU2)
-
brenda
Goldman, L.M.; Amyes, T.L.; Goryanova, B.; Gerlt, J.A.; Richard, J.P.
Enzyme architecture deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase
J. Am. Chem. Soc.
136
10156-10165
2014
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae ATCC 204508 / S288c (P03962)
brenda
Reyes, A.C.; Amyes, T.L.; Richard, J.P.
Enzyme architecture Erection of active orotidine 5'-monophosphate decarboxylase by substrate-induced conformational changes
J. Am. Chem. Soc.
139
16048-16051
2017
Saccharomyces cerevisiae (P03962), Saccharomyces cerevisiae ATCC 204508 / S288c (P03962)
brenda
Paojinda, P.; Imprasittichai, W.; Krungkrai, S.R.; Palacpac, N.M.Q.; Horii, T.; Krungkrai, J.
Bifunctional activity of fused Plasmodium falciparum orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
Parasitol. Int.
67
79-84
2018
Plasmodium falciparum (Q8T6J6), Plasmodium falciparum
brenda