Information on EC 4.1.1.23 - Orotidine-5'-phosphate decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.1.23
-
RECOMMENDED NAME
GeneOntology No.
Orotidine-5'-phosphate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
nitrogen ylide mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
catalytic mechanism with freely reversible binding, a very limited contribution to the overall rate is made by chemical steps preceding decarboxylation
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
reaction mechanism
P25971
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
reaction mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
kinetic mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
catalytic mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
catalytic mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
catalytic mechanism
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism, thermodynamic data
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
decarboxylation mechanism, substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
direct decarboxylation mechanism, modeling with 6-carbanion derivatives of uracil analogues, overview
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
reaction mechanism involving the active site aspartate residue Asp91, electrostatic stress furnishes the majority of the catalytic driving force for OMP decarboxylation, ylide generation is not the rate-limiting step in the ODCase reaction
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
catalytic mechanism
Saccharomyces cerevisiae BJ5424
-
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
Saccharomyces cerevisiae BJ5464
-
-
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
nitrogen ylide mechanism
Saccharomyces cerevisiae 15C
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Pyrimidine metabolism
-
-
pyrimidine metabolism
-
-
UMP biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
orotidine-5'-phosphate carboxy-lyase (UMP-forming)
The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Decarboxylase, orotidine 5'-phosphate
-
-
-
-
ODCase
-
-
-
-
OMP decarboxylase
-
-
-
-
OMP-DC
-
-
-
-
OMPDCase
-
-
-
-
OMPdecase
-
-
-
-
Orotate decarboxylase
-
-
-
-
Orotate monophosphate decarboxylase
-
-
-
-
Orotic decarboxylase
-
-
-
-
Orotidine 5'-monophosphate decarboxylase
-
-
-
-
Orotidine 5'-phosphate decarboxylase
-
-
-
-
Orotidine monophosphate decarboxylase
-
-
-
-
Orotidine phosphate decarboxylase
-
-
-
-
Orotidine-5'-monophosphate decarboxylase
-
-
-
-
Orotidylate decarboxylase
-
-
-
-
Orotidylic acid decarboxylase
-
-
-
-
Orotidylic decarboxylase
-
-
-
-
Orotodylate decarboxylase
-
-
-
-
UMP synthase
-
-
-
-
Uridine 5'-monophosphate synthase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-62-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
theoretical study based on the structure of Bacillus subtilis enzyme
Uniprot
Manually annotated by BRENDA team
strain NRRL2895(+)
SwissProt
Manually annotated by BRENDA team
Blakeslea trispora NRRL2895(+)
strain NRRL2895(+)
SwissProt
Manually annotated by BRENDA team
strain K-12 harboring the cloned pyrF gene on the multicopy plasmid pDK26
-
-
Manually annotated by BRENDA team
bifunctional UMP synthase contains activities of EC 2.4.2.10 and EC 4.1.1.23
-
-
Manually annotated by BRENDA team
Methanobacterium thermoautotrophicus
-
UniProt
Manually annotated by BRENDA team
Methanobacterium thermoautotrophicus DSM 1053
-
UniProt
Manually annotated by BRENDA team
Methanococcus thermoautotrophicum
-
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicus DSM 1053
-
UniProt
Manually annotated by BRENDA team
bifunctional UMP synthase contains activities of EC 2.4.2.10 and EC 4.1.1.23
-
-
Manually annotated by BRENDA team
gene pyrG; gene pyrG
UniProt
Manually annotated by BRENDA team
no activity in Treponema pallidum
-
-
-
Manually annotated by BRENDA team
isolate 3D7
UniProt
Manually annotated by BRENDA team
strain BJ5464
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae 15C
strain 15C
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae BJ5424
strain BJ5424
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae BJ5464
strain BJ5464
-
-
Manually annotated by BRENDA team
; strain DG6, ATCC 49426
-
-
Manually annotated by BRENDA team
Sulfolobus acidocaldarius DG6
; strain DG6, ATCC 49426
-
-
Manually annotated by BRENDA team
strain ATCC 35405, single copy gene pyrF or TDE2110
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(beta-D-erythrofuranosyl)-5-fluoroorotic acid
? + CO2
show the reaction diagram
-
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)orotic acid
?
show the reaction diagram
-
truncated substrate
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
show the reaction diagram
-
decreased catalytic rate compared with orotidine 5'-phosphate as substrate
-
?
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
show the reaction diagram
P03962
less effective than orotidine 5-phosphate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
-
-
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
show the reaction diagram
-
50% reduced kcat-value compared with orotidine 5'-phosphate as substrate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
show the reaction diagram
-
nearly equally effective as orotidine 5'-phosphate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
show the reaction diagram
-
partially active substrate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5424
-
nearly equally effective as orotidine 5'-phosphate
-
?
5'-deoxy-5-fluoroorotidine
? + CO2
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
-
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
-
-
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
5-Fluoroorotidine 5'-phosphate
5-Fluorouridine 5'-phosphate + CO2
show the reaction diagram
-
the 5-fluoro substituent results in a 3400fold increase in the first-order rate constant for deuterium exchange
-
-
?
6-cyano-UMP
6-hydroxyuridine 5'-phosphate + UMP
show the reaction diagram
-
-
-
-
?
6-cyano-UMP
beta-D-ribofuranosylbarbiturate 5'-monophosphate
show the reaction diagram
-
hydrolysis
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
show the reaction diagram
-
-
-
-
?
orotic acid
?
show the reaction diagram
P03962
extremely poor substrate
-
?
orotidine
uridine + CO2
show the reaction diagram
-
low decarboxylation activity
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q8T6J6
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q8IJH3
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q870M2
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Methanococcus thermoautotrophicum
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q2HZ31
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
B3GF12
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q26232
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Methanobacterium thermoautotrophicus
O26232
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
absolutely specific
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
mechanism
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalytic mechanism involving protonation at O2 and a proposed Zn2+ interaction at O4, role of Lys-93 in catalysis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P25971
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
show the reaction diagram
-
catalytic mechanism, role of Lys-93 in catalysis, enzyme structure
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
enzyme has two functionally independent substrate binding sites
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
P03962
enzyme/active site structure, mode of substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
mechanism, enzyme structure
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
mechansim, no formation of a vinyl anion intermediate, enzyme structure, the active sites are located at the dimer interface
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
catalyzes the critical final step in the pyrimidine biosynthetic pathway
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the final step in the de novo biosynthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P25971
catalyzes the final step in the de novo biosynthesis of uridine monophosphate
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P03962
catalyzes the final step of pyrimidine biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the last step in the de novo synthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the last step of de novo pyrimidine synthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q870M2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
last step in the biosynthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
last step in the de novo synthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
the sixth enzyme in the pathway catalyzing formation of uridine 5'-monophosphate
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is required for de novo pyrimidine synthesis catalyzing the key final step in de novo synthesis of UMP
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
the enzyme is the most effective pure protein catalyst known in nature
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P11172
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P11172
the decarboxylase shows an extremely fast rate acceleration
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q8IJH3
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
show the reaction diagram
O26232
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
show the reaction diagram
Methanobacterium thermoautotrophicus DSM 1053
O26232
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Methanothermobacter thermautotrophicus DSM 1053
O26232
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
show the reaction diagram
Saccharomyces cerevisiae BJ5424
-
catalytic mechanism involving protonation at O2 and a proposed Zn2+ interaction at O4, role of Lys-93 in catalysis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5424
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5464
-
mechanism, catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae 15C
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae 15C
-
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Blakeslea trispora NRRL2895(+)
Q870M2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Sulfolobus acidocaldarius DG6
-
-
-
?
Orotidine 5'-phosphate
?
show the reaction diagram
-
final step in pyrimidine biosynthesis
-
-
-
Orotidine 5'-phosphate
?
show the reaction diagram
-
final step in pyrimidine biosynthesis
-
-
-
Orotidine 5'-phosphate
?
show the reaction diagram
-
required for the biosynthesis of uridylic acid
-
-
-
orotidine 5'-phosphate + H+
UMP + CO2
show the reaction diagram
-
-
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
show the reaction diagram
-
pseudohydrolysis process
-
-
?
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
-
?
additional information
?
-
-
not: 2-thioorotidine 5-phosphate, undetectable activity with CMP-6-carboxylate and weak binding to ODCase
-
?
additional information
?
-
P25971
theoretical studies of the effect of thio substitution on orotidine monophosphate decarboxylase substrates
-
-
-
additional information
?
-
-
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
-
additional information
?
-
Q2HZ31
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
-
additional information
?
-
-
the enzyme also converts 6-cyano-UMP to barbituric acid monophosphate with low activity
-
-
-
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
?
-
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
?
-
-
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 ECS 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
?
-
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
?
-
Saccharomyces cerevisiae BJ5424
-
not: 2-thioorotidine 5-phosphate, undetectable activity with CMP-6-carboxylate and weak binding to ODCase
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q8IJH3
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Plasmodium vivax, Methanococcus thermoautotrophicum
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q2HZ31
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
B3GF12
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q26232
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the critical final step in the pyrimidine biosynthetic pathway
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the final step in the de novo biosynthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P25971
catalyzes the final step in the de novo biosynthesis of uridine monophosphate
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P03962
catalyzes the final step of pyrimidine biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the last step in the de novo synthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
catalyzes the last step of de novo pyrimidine synthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Q870M2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
last step in the biosynthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
last step in the de novo synthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
the sixth enzyme in the pathway catalyzing formation of uridine 5'-monophosphate
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is required for de novo pyrimidine synthesis catalyzing the key final step in de novo synthesis of UMP
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
-
the enzyme is the most effective pure protein catalyst known in nature
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
P11172
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
?
show the reaction diagram
-
final step in pyrimidine biosynthesis
-
-
-
Orotidine 5'-phosphate
?
show the reaction diagram
-
final step in pyrimidine biosynthesis
-
-
-
Orotidine 5'-phosphate
?
show the reaction diagram
-
required for the biosynthesis of uridylic acid
-
-
-
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5424
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5424
-
production of UMP, the biosynthetic precursor of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Saccharomyces cerevisiae BJ5464
-
catalyzes the final step of de novo pyrimidine nucleotide biosynthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Blakeslea trispora NRRL2895(+)
Q870M2
last common step in pyrimidine biosynthesis, constitutive expression
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Sulfolobus acidocaldarius DG6
-
-
-
?
additional information
?
-
-
the enzyme is required for 5-fluoroorotic acid toxicity
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
additional information
-
functions without cofactors
-
additional information
-
no cofactor requirement
-
additional information
-
no cofactors are involved in catalysis
-
additional information
-
no cofactor requirement
-
additional information
-
no cofactors
-
additional information
P25971
no cofactor requirement
-
additional information
-
no cofactor required
-
additional information
-
no cofactors required
-
additional information
-
ODCase contains no small molecule cofactors
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
-
zinc, rather than a proton may be largely responsible for neutralizing charge development in the transition state for OMP decarboxylation
Zinc
-
no zinc detected
Zn2+
-
mechanism may include participation of Zn2+, which interacts at O4 with the substrate
Zn2+
-
native ODCase expressed in yeast contains zinc, but not recombinant ODCase expressed in Escherichia coli, zinc is not involved in substrate decarboxylation
additional information
-
no metal cofactor, e.g. Zn2+ or other transition metal ions
additional information
-
no metal cofactor
additional information
-
no metal ion requirement
additional information
-
no metal ion requirement
additional information
-
functions without metals
additional information
-
metal-independent reaction
additional information
-
no metal ion requirement
additional information
-
no metals are involved in catalysis
additional information
-
zinc-free fully active recombinant ODCase expressed in Escherichia coli, metals do not directly participate in the decarboxylation mechanism
additional information
-
no metal cofactor requirement
additional information
-
no metals
additional information
-
no metal ion required
additional information
-
no metals required
additional information
-
ODCase contains no metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
Q8IJH3
i.e. CMP-N3-oxide
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-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
mode of binding
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
-
1-methylorotate
-
modeling of binding and structure
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-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-bromo-UMP
-
-
5-Bromoorotidylate
-
-
5-Chloroorotidylate
-
-
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
5-fluoro-UMP
-
-
5-fluoro-UMP
-
-
5-fluorouracil
-
1 mM, 14% inhibition
5-iodo-UMP
-
-
5-phosphoribofuranosylallopurinol
-
-
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
poor inhibitor
6-amino-1-methyluracil
-
modeling of binding and structure
6-amino-5-fluorouridine
-
competitive inhibition at submicromolar concentrations
6-amino-UMP
-
competitive inhibition
6-amino-uridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-monophosphate
-
-
6-aminouridine 5'-phosphate
-
-
6-aza-UMP
-
competitive inhibition
6-aza-uridine 5'-monophosphate
-
-
6-Azauracil
-
competitive inhibitor
6-azauridine 5'-monophosphate
Bacillus subtilis, Escherichia coli, Homo sapiens, Methanococcus thermoautotrophicum
-
-
6-azauridine 5'-monophosphate
-
-
6-azauridine 5'-monophosphate
-
-
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-azauridine 5'-phosphate
-
mode of binding
6-azauridine 5'-phosphate
-
-
6-azido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
6-azido-5-fluorouridine
-
irreversible inhibitor
6-azido-uridine 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
-
reversible inhibitor
6-cyano-UMP
-
competitive inhibition
6-cyano-uridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-monophosphate
-
-
6-cyanouridine 5'-phosphate
-
competitive
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-hydroxymethyl-UMP
-
-
6-hydroxyUMP
-
a transition state analogue inhibitor, binding structure in complex with the enzyme, overview
6-hydroxyuridine
-
potent inhibitor
6-hydroxyuridine 5'-monophosphate
-
tightly binding competitive inhibitor
6-hydroxyuridine 5'-phosphate
-
potent competitive inhibitor
6-hydroxyuridine 5'-phosphate
-
mode of binding
6-hydroxyuridine 5'-phosphate
-
-
6-iodo-UMP
-
-
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
-
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-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
-
6-iodouridine 5'-monophosphate
-
irreversible inhibitor
6-methyl-uridine
-
-
6-methyl-uridine 5'-monophosphate
-
-
6-methyluridine 5'-phosphate
-
-
6-thiocarboxamidouridine
-
potent inhibitor
6-thiocarboxamidouridine 5'-monophosphate
-
-
6-thiocarboxamidouridine 5'-phosphate
-
-
6-thiocarboxamidouridine 5'-phosphate
-
competitive, very strong, reversible inhibition
7-Ribosyloxipurinol 5'-phosphate
-
-
8-azaxanthosine 5'-phosphate
-
-
allopurinol beta-D-riboside 5'-phosphate
-
-
allopurinol-3-riboside 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
CMP
-
weak inhibitor
CMP
Q8IJH3
weak inhibitor
Dimethylsulfoxide
-
20% v/v, 8% inhibition
EDTA
-
10 mM, 6% inhibition; 10 mM, at 70C, weak inhibition
guanidine hydrochloride
-
2 M, denaturates
Guanidine-HCl
-
2.0 M, complete inhibition
Guanidinium chloride
-
1 M, at 70C, 81.4% inhibition
nifedipine
-
competitive inhibitor
nimodipine
-
competitive inhibitor
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
-
-
phosphate
-
weak
phosphate
-
low activity in phosphate buffers, inhibitory or destabilizing effect
phosphate
-
competitive, mutant enzyme C155S
potassium phosphate
-
-
pyrazofurin 5'-monophosphate
Bacillus subtilis, Escherichia coli, Homo sapiens, Methanococcus thermoautotrophicum
-
-
pyrazofurin 5'-monophosphate
-
-
pyrazofurin 5'-monophosphate
-
-
ribose 5'-phosphate
-
-
ribose 5-phosphate
-
competitive inhibitor
ribose 5-phosphate
-
-
SDS
-
1%, at 70C, complete inactivation; 1%, complete inhibition
thiopurinol 5'-phosphate
-
-
UMP
-
product inhibition
UMP
-
competitive
UMP
-
-
UMP
-
ineffective inhibitor
UMP
-
weak inhibitor
UMP
-
competitive inhibition
UMP
-
1 mM, 19% inhibition; 1 mM, at 70C, 19% inhibition
Uracil
-
strong feedback inhibition
xanthosine 5'-monophosphate
Bacillus subtilis, Escherichia coli, Homo sapiens, Methanococcus thermoautotrophicum
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-monophosphate
-
-
xanthosine 5'-phosphate
-
competitive inhibition
xanthosine 5'-phosphate
-
-
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
-
additional information
-
inhibitor synthesis, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
0.1 mM, 2.2fold stimulation
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.1 mM, at 70C, 2.2fold activation
6-Azauracil
-
1 mM, 1.2fold activation
HPO32-
-
decarboxylation of substrate analog 5'-deoxy-5-fluoroorotidine is activated. Decarboxylation of truncated substrate analog 1-(beta-D-erythrofuranosyl)-5-fluoroorotic acid is activated by exogenous phosphite dianion, but the 5-F substituent results in only a 0.8 kcal stabilization of the transition state for the phosphite-activated reaction
N-ethylmaleimide
-
10 mM, 18fold stimulation; 10 mM, at 70C, 17.8fold activation
orotidine 5'-phosphate
-
the 5'-phosphate group of the substrate activates the enzyme 240000000fold. The binding of orotidine 5'-monophosphate is accompanied by a conformational change of the enzyme from an open, inactive conformation to a closed, active conformation. As the substrate traverses the reaction coordinate to form the stabilized vinyl carbanion/carbene intermediate, interactions that destabilize the carboxylate group of the substrate and stabilize the intermediate are enforced. The activation is equivalently described by an intrinsic binding energy of 11.4 kcal/mol. The residues that directly contact the 5'-phosphate group, participate in a hydrophobic cluster near the base of the active site loop that sequesters the bound substrate from the solvent, or that form hydrogen bonding interactions across the interface between the mobile and fixed half-barrel domains of the (beta/alpha)8-barrel structure. The data support a model in which the intrinsic binding energy provided by the 5'-phosphate group is used to allow interactions both near the N-terminus of the active site loop and across the domain interface that stabilize the complexes of the enzyme in the active closed conformation with the substrate or with the substrate intermediate with the destabilized carboxylate group relative to the complex of the enzyme in the open inactive conformation with the substrate
phosphite dianion
-
activates
Uracil
-
1 mM, 1.3fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, T100A mutant
0.0054
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, wild-type enzyme
0.008
2'-deoxyorotidine 5'-phosphate
-
wild-type enzyme
0.01
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, D37A mutant
0.02
4-Thioorotidine 5'-phosphate
-
-
0.03
5-Azaorotidine 5'-phosphate
-
-
0.0008
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
0.0082
5-Fluoroorotidine 5'-phosphate
-
wild type enzyme
0.056
5-Fluoroorotidine 5'-phosphate
-
-
0.058
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C
0.0007
Orotidine
-
pH 7.2, 23C, mutant enzyme C155S
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, 25C
0.00026
orotidine 5'-phosphate
-
orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase, 20C
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
-
22-25C, 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, 37C
0.0007
orotidine 5'-phosphate
-
pH 6, 25C
0.0007
orotidine 5'-phosphate
-
-
0.0007
orotidine 5'-phosphate
-
pH 7.2, 25C, wild-type enzyme
0.0007
orotidine 5'-phosphate
-
pH 7, 25C
0.0007
orotidine 5'-phosphate
-
22C, native ODCase expressed in yeast
0.0007
orotidine 5'-phosphate
-
wild-type enzyme
0.001 - 0.002
orotidine 5'-phosphate
-
Km value is very dependent on the NaCl concentration, NaCl increases the Km value
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, 25C
0.0012
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25C
0.0013
orotidine 5'-phosphate
-
-
0.0014
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
0.0015
orotidine 5'-phosphate
-
-
0.0016
orotidine 5'-phosphate
-
solubilized enzyme
0.0016
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
wild-type, pH 7.1, 25C
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 22C
0.0018
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
0.0023
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant I96T, pH 7.1, 25C
0.0028
orotidine 5'-phosphate
-
wild-type, pH 7.2, 25C
0.003
orotidine 5'-phosphate
-
dimeric enzyme form
0.003
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123S, pH 7.1, 25C
0.0032
orotidine 5'-phosphate
-
pH 8.0, 37C
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, 25C
0.0035
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123N, pH 7.1, 25C
0.0037
orotidine 5'-phosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
0.0041
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25C
0.0042
orotidine 5'-phosphate
-
pH 7.2, 25C, D37A mutant
0.0046
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant V155D, pH 7.1, 25C
0.0047
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant V155S, pH 7.1, 25C
0.0048
orotidine 5'-phosphate
-
-
0.005
orotidine 5'-phosphate
-
-
0.005
orotidine 5'-phosphate
-
pH 7.5, 55C
0.005
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25C
0.0053
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25C
0.0055
orotidine 5'-phosphate
-
mutant Y206F, pH 7.1, 25C
0.006
orotidine 5'-phosphate
-
-
0.006
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant D70N, pH 7.1, 25C
0.0067
orotidine 5'-phosphate
-
pH 7.2, 25C, T100A mutant
0.0075
orotidine 5'-phosphate
-
membrane-bound enzyme
0.008 - 0.009
orotidine 5'-phosphate
-
-
0.00991
orotidine 5'-phosphate
-
-
0.0134
orotidine 5'-phosphate
-
monofunctional enzyme expressed in Escherichia coli
0.0166
orotidine 5'-phosphate
-
-
0.024
orotidine 5'-phosphate
-
mutant V182A, pH 7.1, 25C
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, 25C
0.033
orotidine 5'-phosphate
-
mutant T159V, pH 7.1, 25C
0.036
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25C
0.1 - 1
orotidine 5'-phosphate
-
mutant Q185A, pH 7.1, 25C
0.1
orotidine 5'-phosphate
-
mutant V182A/Y206F, pH 7.1, 25C
0.13
orotidine 5'-phosphate
-
mutant R160A/Y206F, pH 7.1, 25C
0.3
orotidine 5'-phosphate
-
mutant T159V/Y206F, pH 7.1, 25C
0.6
orotidine 5'-phosphate
-
mutant R160A/V182A, pH 7.1, 25C
0.64
orotidine 5'-phosphate
-
K59A mutant
0.7
orotidine 5'-phosphate
-
mutant T159V/V182A, pH 7.1, 25C
0.73
orotidine 5'-phosphate
-
K59A mutant
0.98
orotidine 5'-phosphate
-
mutant R203A, pH 7.1, 25C
1.4
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C
1.9
orotidine 5'-phosphate
-
mutant T159V/V182A/Y206F, pH 7.1, 25C
30
orotidine 5'-phosphate
-
value is higher than 30 mM, pH 7.2, 23C, mutant enzyme C155S
0.41
5-Fluoroorotidine 5'-phosphate
-
K59A mutant
additional information
additional information
-
kinetic properties, catalytic proficiency/efficiency
-
additional information
additional information
-
kinetic data and mechanism
-
additional information
additional information
-
kinetics, most proficient enzyme known
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, D37A mutant
0.15
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, wild-type enzyme
0.16
2'-deoxyorotidine 5'-phosphate
-
pH 7.2, 25C, T100A mutant
9
4-Thioorotidine 5'-phosphate
-
-
5
5-Azaorotidine 5'-phosphate
-
-
29
5-Fluoroorotidine 5'-phosphate
-
K59A mutant
92
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C, presence of 0.1 M NaCl
95
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25C, presence of 0.1 M NaCl
242
5-Fluoroorotidine 5'-phosphate
-
wild type enzyme
22
Orotidine
-
pH 7.2, 23C, mutant enzyme C155S
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, 23C, mutant enzyme C155S
0.00023
orotidine 5'-phosphate
-
below, D96A mutant
0.0005
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant V155D, pH 7.1, 25C
0.01 - 1
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant I96S, pH 7.1, 25C; mutant V155S, pH 7.1, 25C
0.024
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant D70N, pH 7.1, 25C
0.24
orotidine 5'-phosphate
-
mutant T159V/V182A/Y206F, pH 7.1, 25C
0.34
orotidine 5'-phosphate
-
K59A mutant
0.36
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123S, pH 7.1, 25C
0.5
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25C
0.52
orotidine 5'-phosphate
-
K59A mutant
0.56
orotidine 5'-phosphate
-
mutant T159V/V182A, pH 7.1, 25C
0.64
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123N, pH 7.1, 25C
0.69
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant I96T, pH 7.1, 25C
0.7
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25C
0.75
orotidine 5'-phosphate
-
-
0.9
orotidine 5'-phosphate
-
pH 7.2, 25C, D37A mutant
1
orotidine 5'-phosphate
-
mutant R160A/V182A, pH 7.1, 25C
1
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C, presence of 0.1 M NCl
1.1
orotidine 5'-phosphate
-
mutant R160A/Y206F, pH 7.1, 25C; mutant T159V/Y206F, pH 7.1, 25C
1.4
orotidine 5'-phosphate
-
mutant Q185A, pH 7.1, 25C
1.5
orotidine 5'-phosphate
-
mutant R203A, pH 7.1, 25C; mutant V182A/Y206F, pH 7.1, 25C
2 - 8
orotidine 5'-phosphate
-
pH 7, constant above pH 7, declines below pH 7
2
orotidine 5'-phosphate
-
mutant R160A, pH 7.1, 25C
2.3
orotidine 5'-phosphate
-
mutant T159V, pH 7.1, 25C
3
orotidine 5'-phosphate
-
mutant V182A, pH 7.1, 25C
3.2
orotidine 5'-phosphate
-
mutant T80S, pH 7.2, 25C
4
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
wild-type, pH 7.1, 25C
4.1
orotidine 5'-phosphate
-
mutant Y206F, pH 7.1, 25C
5.3
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
6.7
orotidine 5'-phosphate
-
-
7.2
orotidine 5'-phosphate
-
pH 7.2, 25C, T100A mutant
7.5
orotidine 5'-phosphate
-
monofunctional enzyme expressed in Escherichia coli
8.1
orotidine 5'-phosphate
-
-
13
orotidine 5'-phosphate
-
22C, native ODCase expressed in yeast
13.7
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25C
14 - 20
orotidine 5'-phosphate
-
pH 7.2, 25C, not affected by NaCl concentration
14.4
orotidine 5'-phosphate
-
mutant D22G, pH 7.2, 25C
15
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C, presence of 0.1 M NaCl
15.6
orotidine 5'-phosphate
-
pH 8.0, 37C
19
orotidine 5'-phosphate
-
-
19
orotidine 5'-phosphate
-
22-25C, pH 7.2, recombinant ODCase expressed in Escherichia coli
20.7
orotidine 5'-phosphate
-
-
21
orotidine 5'-phosphate
-
pH 7.5, 55C
22
orotidine 5'-phosphate
-
wild type enzyme
24.6
orotidine 5'-phosphate
-
multienzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
27
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25C
29.7
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25C
41
orotidine 5'-phosphate
-
Q215A mutant
42
orotidine 5'-phosphate
-
wild-type, pH 7.2, 25C
44
orotidine 5'-phosphate
-
pH 7.2, 25C, wild-type enzyme
44
orotidine 5'-phosphate
-
wild-type enzyme
570
5-Fluoroorotidine 5'-phosphate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
very proficient enzyme
-
additional information
additional information
-
very high catalytic proficiency
-
additional information
additional information
-
highly proficient enzyme
-
additional information
additional information
-
high catalytic proficiency
-
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
-
remarkable catalytic power
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/Y217F/R235A, pH 7.1, 25C
0
4.2
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/R235A, pH 7.1, 25C
0
4.6
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A/Y217F, pH 7.1, 25C
0
10
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Y217F/R235A, pH 7.1, 25C
0
11
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Q215A, pH 7.1, 25C
0
12
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant Y217F, pH 7.1, 25C
0
26
1-(beta-D-erythrofuranosyl)orotic acid
-
mutant R235A, pH 7.1, 25C; wild-type, pH 7.1, 25C
0
160
5-Fluoroorotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C
9073
12000
5-Fluoroorotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
9073
0.00004
orotidine 5'-phosphate
-
mutant Q215A/Y217F/R235A, pH 7.1, 25C
742
0.0041
orotidine 5'-phosphate
-
mutant Y217F/R235A, pH 7.1, 25C
742
0.013
orotidine 5'-phosphate
-
mutant Q215A/R235A, pH 7.1, 25C
742
0.13
orotidine 5'-phosphate
-
mutant T159V/V182A/Y206F, pH 7.1, 25C
742
0.46
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant V155D, pH 7.1, 25C
742
0.61
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C
742
0.8
orotidine 5'-phosphate
-
mutant T159V/V182A, pH 7.1, 25C
742
0.91
orotidine 5'-phosphate
-
mutant R235A, pH 7.1, 25C
742
1.5
orotidine 5'-phosphate
-
mutant R203A, pH 7.1, 25C
742
1.7
orotidine 5'-phosphate
-
mutant R160A/V182A, pH 7.1, 25C
742
2.3
orotidine 5'-phosphate
-
mutant Q215A/Y217F, pH 7.1, 25C
742
3.7
orotidine 5'-phosphate
-
mutant T159V/Y206F, pH 7.1, 25C
742
4
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant D70N, pH 7.1, 25C
742
8.5
orotidine 5'-phosphate
-
mutant R160A/Y206F, pH 7.1, 25C
742
10
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant I96S, pH 7.1, 25C
742
13
orotidine 5'-phosphate
-
mutant Q185A, pH 7.1, 25C
742
14
orotidine 5'-phosphate
-
mutant D71C, pH 7.2, 25C
742
15
orotidine 5'-phosphate
-
mutant V182A/Y206F, pH 7.1, 25C
742
22
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant V155S, pH 7.1, 25C
742
67
orotidine 5'-phosphate
-
mutant R160A, pH 7.1, 25C
742
70
orotidine 5'-phosphate
-
mutant T159V, pH 7.1, 25C
742
120
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123S, pH 7.1, 25C
742
130
orotidine 5'-phosphate
-
mutant V182A, pH 7.1, 25C
742
170
orotidine 5'-phosphate
-
mutant D76C, pH 7.2, 25C
742
180
orotidine 5'-phosphate
-
mutant Y217F, pH 7.1, 25C
742
190
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant L123N, pH 7.1, 25C
742
260
orotidine 5'-phosphate
-
mutant Q215A, pH 7.1, 25C
742
300
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
mutant I96T, pH 7.1, 25C
742
750
orotidine 5'-phosphate
-
mutant Y206F, pH 7.1, 25C
742
2000
orotidine 5'-phosphate
Methanobacterium thermoautotrophicus
-
wild-type, pH 7.1, 25C
742
2900
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
742
4500
orotidine 5'-phosphate
-
mutant D22G, pH 7.2, 25C
742
5100
orotidine 5'-phosphate
-
mutant L130M, pH 7.2, 25C
742
5900
orotidine 5'-phosphate
-
mutant V167N, pH 7.2, 25C
742
11000
orotidine 5'-phosphate
-
wild-type, pH 7.1, 25C
742
12000
orotidine 5'-phosphate
-
mutant Q201H, pH 7.2, 25C
742
15000
orotidine 5'-phosphate
-
mutant T80S, pH 7.2, 25C; wild-type, pH 7.2, 25C
742
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.022
(5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate
Q8IJH3
pH 7.5, 22C
0.028
(5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate
-
pH 7.5, 22C
0.00001
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
below
0.26
2'-deoxyuridine 5'-phosphate
-
pH 7.4, 25C
0.043
2-thiouridine 5'-phosphate
-
pH 7, 25C
0.015
4-thiouridine 5'-phosphate
-
pH 7, 25C
0.0208
5,6-dihydro-6-sulfonyl-OMP
-
pH 7.2
0.0292
5,6-dihydro-6-sulfonyl-UMP
-
pH 7.2
0.36
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.759
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
9.1
5-cyano-UMP
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
290
5-cyano-UMP
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
550
5-cyano-UMP
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
0.67
5-fluoro-UMP
-
-
3.322
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
4
6-amido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
Ki above 4 mM, in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.00084
6-amino-UMP
-
pH 7.5, 55C
0.0021
6-amino-uridine 5'-monophosphate
-
-
0.00084
6-aminouridine 5'-monophosphate
-
-
0.00084
6-aminouridine 5'-phosphate
-
-
0.0124
6-aza-UMP
-
pH 7.5, 55C
0.14
6-aza-UMP
-
-
0.0011
6-aza-uridine 5'-monophosphate
-
-
0.000012
6-azauridine 5'-monophosphate
-
-
0.000029
6-azauridine 5'-phosphate
-
Q215A mutant
0.000036
6-azauridine 5'-phosphate
-
wild-type enzyme
0.000064
6-azauridine 5'-phosphate
-
-
0.000064
6-azauridine 5'-phosphate
-
pH 7.4, 25C, wild-type enzyme
0.000093
6-azauridine 5'-phosphate
-
-
0.0077
6-azauridine 5'-phosphate
-
pH 7.4, 25C, D37A mutant
0.0094
6-azauridine 5'-phosphate
-
pH 7.4, 25C, T100A mutant
0.0124
6-azauridine 5'-phosphate
-
-
0.039
6-azauridine 5'-phosphate
-
K59A mutant
0.002
6-azido-uridine 5'-monophosphate
-
-
0.00019
6-azidouridine 5'-monophosphate
-
-
0.002
6-azidouridine 5'-monophosphate
-
-
0.00019
6-azidouridine 5'-phosphate
-
-
0.00132
6-carbamoyl-UMP
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.037
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
2
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
Ki above 2 mM, in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.029
6-cyano-UMP
-
pH 7.5, 55C
0.026
6-cyano-uridine 5'-monophosphate
-
-
0.0286
6-cyanouridine
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.204
6-cyanouridine
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55C
0.011
6-cyanouridine 5'-phosphate
-
-
0.029
6-cyanouridine 5'-phosphate
-
-
0.000000008
6-hydroxyuridine 5'-phosphate
-
wild-type enzyme
0.0000000088
6-hydroxyuridine 5'-phosphate
-
-
0.000094
6-hydroxyuridine 5'-phosphate
-
K59A mutant
0.0341
6-methyl-uridine 5'-monophosphate
-
-
0.134
6-methyluridine 5'-phosphate
-
-
0.0000035
6-thiocarboxamidouridine 5'-phosphate
-
recombinant ODCase expressed in Escherichia coli
0.00012
8-azaxanthosine 5'-phosphate
-
-
0.004
allopurinol beta-D-riboside 5'-phosphate
-
-
0.00024
allopurinol-3-riboside 5'-monophosphate
-
-
4.3
AMP
-
-
0.000000009
barbiturate ribonucleoside 5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
1.4
CMP
-
-
1.4
CMP
-
pH 7.5, 22C
7.4
dAMP
-
-
0.000052
oxypurinol 5'-phosphate
-
-
0.7
phosphate
-
mutant enzyme C155S
0.0000036
pyrazofurin 5'-monophosphate
-
-
0.000005
pyrazofurin-5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
0.000017
pyrazofurin-5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
0.00013
pyrazofurin-5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
0.0062
pyrazofurin-5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22C
37
ribose
-
pH 7.4, 25C
0.081
ribose 5'-phosphate
-
pH 7.4, 25C
0.08
ribose 5-phosphate
-
-
0.5
ribose 5-phosphate
-
-
0.0025
thiopurinol 5'-phosphate
-
-
8.7
TMP
-
-
0.092
UMP
-
pH 7, 25C
0.17
UMP
-
Q215A mutant
0.2 - 0.4
UMP
-
-
0.2
UMP
-
pH 7.4, 25C, wild-type enzyme
0.2
UMP
-
wild-type enzyme
0.21
UMP
-
pH 7.4, 25C, D37A mutant
0.21
UMP
Q8IJH3
pH 7.5, 22C
0.22
UMP
-
-
0.22
UMP
-
pH 7.5, 22C
0.33
UMP
-
K59A mutant
0.37
UMP
-
pH 7.4, 25C, T100A mutant
0.5
UMP
-
-
0.0000044
xanthosine 5'-monophosphate
-
-
0.00041
xanthosine 5'-phosphate
-
pH 7.4, 25C, wild-type enzyme
0.00041
xanthosine 5'-phosphate
-
wild-type enzyme
0.00046
xanthosine 5'-phosphate
-
Q215A mutant
0.012
xanthosine 5'-phosphate
-
pH 7.4, 25C, T100A mutant
0.024
xanthosine 5'-phosphate
-
-
0.039
xanthosine 5'-phosphate
-
pH 7.4, 25C, D37A mutant
0.73
xanthosine 5'-phosphate
-
K59A mutant
0.0007
XMP
-
-
7.2
IMP
-
-
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics, isothermal calorimetry
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
5-bromo-UMP
-
-
0.32
5-fluoro-UMP
-
-
0.25
5-iodo-UMP
-
-
0.45
6-hydroxymethyl-UMP
-
no complete inhibition
0.0044 - 0.0062
6-iodo-UMP
-
pH 7.5, 22C, with different Plasmodium falciparum isolates
0.01
6-iodo-UMP
-
pseudo-IC50 value IUMP is a covalent inhibitor
0.0044
6-iodouridine 5'-monophosphate
-
chloroquine-resistant strain
0.0062
6-iodouridine 5'-monophosphate
-
chloroquine-sensitive strain
0.5305
6-methyl-uridine
-
-
0.4
UMP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00018
-
below, K93A mutant
0.00047
-
below, D96A muatnt
0.00066
-
below, D91A mutant
0.0017
-
-
0.0124
-
pH 8.0, 70C
0.19
-
K59A mutant
10
-
purified recombinant enzyme
12.4
-
pH 8.5, 70C
27.2
-
22C, native ODCase expressed in yeast
39.3
-
22-25C, pH 7.2, recombinant ODCase expressed in Escherichia coli
84
-
Q215A mutant
90
-
wild-type enzyme
additional information
-
enzyme assay
additional information
-
-
additional information
-
same specific activity of native and selenomethionine-substituted ODCase
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
measurement of isotope effects
6.8
-
-
7
-
very sharp
7
-
measurement of carbon isotope effects
7.1
-
activity assay
7.2
-
activity assay
7.4
-
activity assay
7.4
-
activity assay
7.5
-
assay at
7.5
-
activity assay
7.5
-
activity assay
8
-
broad pH-optimum centered about pH 8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
about 50% of maximal acticity at pH 6.0 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
measurement of isotope effects at room temperature
25
-
activity assay
25
-
measurement of carbon isotope effects
25
-
activity assay
37
-
activity assay
37
-
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
Q9C131
calculation from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant mutant ODCase
-
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / PC1)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
Geobacillus kaustophilus (strain HTA426)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Sulfolobus solfataricus (strain 98/2)
Sulfolobus solfataricus (strain 98/2)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
-
multienzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase with two subunits each of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
657769
29500
-
sucrose density gradient centrifugation, at low protein concentration, in absence of ligands that bind at the catalytic site. The enzyme exists as dimer at high protein concentrations
4188
31710
-
-
693556
38000
-
monomer, determined by SDS-PAGE
680570
38000
-
subunit, determined by SDS-PAGE
690945
39850
-
-
693556
46000
-
non-denaturing PAGE
4189
46000
-
gel filtration
651345
51000
-
gel filtration
4172
54000
-
gel filtration
4178
62000
-
gel filtration
4168
62000
-
monomeric enzyme form, gel filtration
4171
64000
-
sucrose density gradient centrifugation, at high protein concentration, in presence of 0.05 mM 6-azauridine 5'-phosphate or 0.002 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid. The enzyme exists as monomer at low protein concentrations
4188
76000
-
active recombinant enzyme, gel filtration
677396
76000
-
active recombinant enzyme, gel filtration; homodimer
680570
76000
-
determined by gel filtration
690945
105000 - 115000
-
bifunctional enzyme that contains activities of EC 2.4.2.10 and EC 4.1.1.23, sucrose density gradient centrifugation with 30% dimethyl sulfoxide and 5% glycerol
4170
115000
-
dimeric enzyme form, gel filtration
4171
250000
-
tetrameric enzyme form, gel filtration
4171
additional information
-
the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase has a MW of 27814, calculation from amino acid sequence
4175
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 27000, about, recombinant ODCase expressed in Escherichia coli, SDS-PAGE
?
Q9C131
x * 31100, calculation from amino acid sequence
?
Q2HZ31
x * 30000, about, sequence calculation
?
Saccharomyces cerevisiae BJ5424
-
x * 27000, about, recombinant ODCase expressed in Escherichia coli, SDS-PAGE
-
dimer
Plasmodium falciparum, Plasmodium vivax, Methanococcus thermoautotrophicum
-
-
dimer
-
2 * 27000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
dimer
-
catalytically active form, substrate-induced enzyme dimerization
dimer
-
each subunit consists of a (beta/alpha)8-barrel, arranged in an antiparallel manner
dimer
-
2 * 38000, active recombinant enzyme, SDS-PAGE
dimer
Sulfolobus acidocaldarius DG6
-
2 * 22000, SDS-PAGE
-
homodimer
-
-
homodimer
-
-
homodimer
-
2 * 22000, SDS-PAGE
homodimer
P25971
active form, subunit structure
homodimer
-
active form, two independently operating active sites per dimer, located at the interface between subunits
homodimer
-
dimer is composed of two alpha/beta-barrels with two shared active sites
multimer
-
orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase form a multienzyme complex with two subunits each of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase (38000 Da per subunit, determined by SDS-PAGE)
homodimer
Sulfolobus acidocaldarius DG6
-
2 * 22000, SDS-PAGE
-
additional information
-
the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase forms a dimer in the presence of ligands
additional information
-
orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase exist as multienzyme complex
additional information
-
QM/MM enzyme simulations, free enzyme and enzyme bound to 6-hydroxy-UMP, QM/MM and metadynamics, enzyme structure analysis, overview
additional information
-
structure-activity analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no posttranslational modifications in recombinant ODCase expressed in Escherichia coli, but presumably in native ODCase from yeast, in which the N-terminus is blocked
additional information
Saccharomyces cerevisiae BJ5424
-
no posttranslational modifications in recombinant ODCase expressed in Escherichia coli, but presumably in native ODCase from yeast, in which the N-terminus is blocked
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
X-ray crystal structure with bound uridine 5-monophosphate
P25971
complexed with the inhibitor 1-(5-phospho-beta-D-ribofuranosyl)barbituric acid
-
uncomplexed apoenzyme and complexed with 1-(5-phospho-beta-D-ribofuranosyl)barbituric acid
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with barbiturate ribonucleoside-5'-monophosphate and 1-(5-monophosphoryl-beta-D-ribofuranos-1-yl)-5-cyanouracil) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
crystal structure in complex with inhibitor (5-(4-amino-3-oxido-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl)-methyl dihydrogen phosphate. Compared to cytosin, the pyrimidine portion exhibits changes in the atomic arrangement. The oxygen atom migrates from N3 to N4 or the C5 position of the cytosine ring. These rearranged nucleotides are each bound to the enzyme in a 2?-endo,syn conformation
-
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with barbiturate ribonucleoside-5'-monophosphate and 1-(5-monophosphoryl-beta-D-ribofuranos-1-yl)-5-cyanouracil) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
nine crystal structures of human OMPD in complex with substrate, product and nucleotide inhibitors are described
-
purified detagged recombinant enzyme, 5 mg/ml protein in 20 mM HEPES-NaOH, pH 7.4, sitting-drop setup, mixing with 0.1 M Tris-HCl, pH 8.0, and 1.8 M (NH4)2SO4 in a 1:1 ratio at 22C, cryoprotection with 20%v/v glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.85-1.92 A resolution, molecular replacement using data from a highly twinned monoclinic crystal, pseudo-merohedrally twinned crystals, overview
-
crystal structures of hydrophobic pocket mutants I96S, I96T, L123N, L123S, V155D, and V155S in the presence of 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid or azaUMP. The interactions of the transition state/vinyl carbanion intermediate with the active site are preserved in each mutant
Methanobacterium thermoautotrophicus
-
crystal structures with ligand anlogues. Enzyme can distort the bond between the aromatic ring of a ligand and its C6 substituent, regardless of the latter's charge or size. The distortion contributes 3.7 kcal/mol to the catalysis. In their respective complexes, 6-methyl-UMP displays significant distortion of its methyl substituent bond, 6-amino-UMP shows the competition between the K72 and C6 substituents for a position close to D70, and the methyl and ethyl esters of orotidine 5'-monophosphate both induce rotation of the carboxylate group substituent out of the plane of the pyrimidine ring. In addition, the bond between the carboxylate group and the pyrimidine ring is distorted
-
eight different crystal forms are grown by the sitting drop method at room temperature for single mutant enzymes liganded with 1-(5-phospho-beta-ribofuranosyl)barbituric acid: Q185A/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid], R203A/[1-(5-phospho-beta-ribofuranosyl)barbituric acid], T159V/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid], T159A/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid], T159S/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid], R160A/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid], Y206F/[1-(5-phospho-beta-ribofuranosyl)barbituric acid], K82A/[1-(5-phospho-beta-D-ribofuranosyl)barbituric acid]; mutants Q185A, R203A, T159V, T159A, T159S, R160A, Y206F, K82A, and double- and triple mutants, to 1.3-1.6 A resolution
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with barbiturate ribonucleoside-5'-monophosphate and 1-(5-monophosphoryl-beta-D-ribofuranos-1-yl)-5-cyanouracil) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
in complex with the inhibitor 6-azauridine 5-phosphate
-
ligand-free ODCase form and complexed with 6-azauridine 5-phosphate
-
native ODCase complexed with 6-azauridine 5'-phosphate, several active site mutants complexed with a variety of ligands, including substrate, product and inhibitors
-
with and without the inhibitor 6-azaUMP, vapour-diffusion method
-
X-ray structure of ODCase complexed with 6-azaorotidine 5-phosphate
-
apo, substrate or product-complex forms of OMPDC, X-ray diffraction structure determination and anaylsis at 2.65-2.7 A; the crystal structures of the apo form of OMPDC, and in complex with OMP and UMP are resolved at resolutions of 2.7, 2.65 and 2.65 A, respectively
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with barbiturate ribonucleoside-5'-monophosphate and 1-(5-monophosphoryl-beta-D-ribofuranos-1-yl)-5-cyanouracil) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
in complex with inhibitor 4-(2-hydroxy-4-methoxyphenyl)-4-oxobutanoic acid, to 2.1 A resolution. 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
-
purified recombinant enzyme, seeding method in a hanging drop, 20C, 10 mg/ml protein in in 50 mM Tris-HCl, pH 8.0, containing 300 mM NaCl and 5 mM dithiothreitol, method optimization, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
the crystal structures of Plasmodium falciparum ODCase in complex with 6-I-UMP, 6-N3-UMP and 6-NH2-UMP are solved at resolutions of 1.95, 1.90 and 1.8 A, respectively
-
the structure of PfODCase is solved to a resolution of 1.5418 A
-
complexed with the inhibitor 6-hydroxyuridine 5-phosphate
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with 4 and 10) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
in complex with 6-hydroxyuridine 5-phosphate
-
in complex with different ligands, e.g. 6-hydroxyuridine 5'-phosphate
-
molecular dynamics simulations on X-ray structure of the enzyme in its free form as well as in complex with ligands 1-(5'-phospho-D-ribofuranosyl) barbituric acid, orotidine 5'-monophosphate, and 6-phosphonouridine 5'-monophosphate
-
orotidine 5'-monophosphate decarboxylase complexed with 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
PDB ID 1DQX, free enzyme and enzyme bound to 6-hydroxy-UMP, crystal structure analysis of the enzyme in presence or absence of a potenial transition state analogue, comparison to predicted structure by QM/MM enzyme simulations, overview
-
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 8.4, 2.12 M ammonium sulfate (enzyme in complex with barbiturate ribonucleoside-5'-monophosphate and 1-(5-monophosphoryl-beta-D-ribofuranos-1-yl)-5-cyanouracil) or using 100 mM Tris-HCl, pH 8.4, 1.4 M ammonium sulfate (enzyme in complex with pyrazofurin-5'-monophosphate)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
26C, 90 min, complete loss of activity. 35% loss of activity after 90 min in presence of azauridine
4178
7.8
-
26C, 90 min, 20% loss of activity
4178
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
half life: 26 min
4169
25
-
orotidine-5'-phosphate decarboxylase activity of UMP synthase, at low protein concentrations remains constant for 40 min
4187
26
-
pH 7.8, 90 min, 20% loss of activity
4178
37
-
half-life: 10 min. Nucleotide inhibitors stabilize against inactivation at 37C
4169
55
-
1 min: 60% loss of the activity of the monomeric form, 10% loss of activity of the tetrameric form
4171
70
-
Tm above 70C
650145
70
-
stable
651345
85
-
in the absence of substrate and product, however, a considerable thermal inactivation was observed at 85C or above; or above, extremely thermostable in presence of substrate or product, considerable thermal inactivation in their absence
651345
90
-
10 min, 90% loss of activity; 10 min, over 90% loss of activity, in absence of substrate and product
651345
additional information
-
the recombinant zinc-free ODCase expressed in Escherichia coli is more thermolabile than the zinc-containing ODCase expressed in yeast
651942
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unliganded enzyme without bound UMP or OMP forms heavy precipitates during purification
P25971
conversion of the monomer to higher molecular weight forms is associated with increased stability
-
Asp-70 makes a crucial contribution to enzyme stability
-
glycerol, 50% v/v is an effective stabilizer of the orotidine-5'-phosphate decarboxylase domain at 4C, -20C or -70C
-
1-ribosyloxipurinol 5'-phosphate prevents loss of activity during preincubation in absence of substrate, when the inhibitor concentration is high enough to inhibit the enzyme substantially
-
NaCl stabilizes the dimeric active enzyme form
-
unstable to repeated freezing and thawing
-
orotidine 5'-phosphate and UMP stabilize
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
at 70C, the enzyme is inactivated by guanidinium chloride at 1 M or higher concentrations
guanidine-HCl
Sulfolobus acidocaldarius DG6
-
at 70C, the enzyme is inactivated by guanidinium chloride at 1 M or higher concentrations
-
SDS
-
at 70C, the enzyme is inactivated by 1% SDS or higher concentrations
SDS
Sulfolobus acidocaldarius DG6
-
at 70C, the enzyme is inactivated by 1% SDS or higher concentrations
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, storage of the high molecular weight forms in presence of 0.15 mM oxipurinol prevents the spontaneous dissociation which occures when these forms are stored in 50 mM potassium phosphate, pH 7.4
-
-70C, dilute buffer plus 2 mM dithiothreitol, purified UMP synthase activity retains orotidine-5'-phosphate decarboxylase activity for several months
-
0C or -70C, 5 mM potassium phosphate, pH 7.0, 2 mM dithiothreitol, rapid loss of orotidine-5'-phosphate decarboxylase activity of the orotidine-5'-phosphate decarboxylase domain of UMP synthase
-
-25C, stable
-
4C, stable for 1 week
-
-20C, 20% glycerol, retention of full activity for more than 2 years
-
0-4C, stable in 10 mM potassium phosphate buffer, pH 5.8-7.5, containing 5 mM 2-mercaptoethanol for several weeks
-
4C, stable for 16 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
P25971
using Affi-Gel Blue chromatography
-
partial
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration
-
using a Ni and a gel filtration column, the His6-tag is removed by thrombin digestion
-
preparation and isolation of the orotidine-5'-phosphate decarboxylase domain of UMP synthase
-
functional recombinant enzyme 300fold from Escherichia coli by nickel affinity chromatography and gel filtration
-
functional recombinant enzyme 300fold from Escherichia coli by nickel affinity chromatography and gel filtration; using a Ni2+-nitrilotriacetic acid-agarose affinity and a Superdex-75 column
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
using a Ni-NTA agarose column, the polyhistidine tag is removed with thrombin, the cleaved protein is further purified using a POROS-HS cation exchange and a Superdex-200 size-exclusion column
-
recombinant ODCase expressed in Escherichia coli
-
recombinant wild-type and mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
P25971
pyrG gene, expression in Mucor circinelloides MU223, sequencing
Q870M2
expression in Escherichia coli
-
expression in Escherichia coli NF 1830, expression of selenomethionine-substituted ODCase in Escherichia coli SO 6733
-
into the plasmid pCAL-n for expression in Escherichia XL1-Blue and BL21DE3 cells
-
expression of His6-tagged GST-fusion enzyme, containing a tobacco etch virus protease site between His6-GST and the target protein, in Escherichia coli
-
into the vector pET15b for expression in Escherichia coli BL21 cells
-
expression in Escherichia coli
-
expression in SKP10 cells
-
expression of the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase in Saccharomyces cerevisiae
-
gene pyrG, DNA and amino acid sequence determination, analysis of 30 untranslated region, promoter region, and coding sequence, genetic organization, a unique OMPD gene of a Sordariomycete that has an intron, sequence comparison, complementation of the uracil auxotrophy of an enzyme-deficient Aspergillus nidulans strain FGSC A722
Q2HZ31
expression in Saccharomyces cerevisiae
Q9C131
expression in Escherichia coli as a monofunctional enzyme form
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
functional enzyme expression in Escherichia coli
-
functional enzyme expression in Escherichia coli; into the vector pTrcHis-TOPO for expression in Escherichia coli TOP10 cells
-
into the vector pET3d for expression in Escherichia coli cells
-
expression in Escherichia coli and Pseudomonas aeruginosa pyrF mutant
-
into the vector pYES2CT
B3GF12
expression of mutant enzymes C155S and D96A/C155S in Escherichia coli
-
ura3 gene expression in Escherichia coli SS6130, expression in yeast
-
ura3 gene, wild-type and mutant ODCase, expression in Escherichia coli SS6130
-
wild-type and mutant ODCase, expression in Escherichia coli SS6130
-
gene pyrF, organization in the pyr operon, DNA and amino acid sequence determination and analysis, expression analysis, expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
D70A
-
inactive active site mutant
D70A/K72A
-
active site double mutant, markedly less stable than native enzyme
D70G
-
active site mutant, markedly less stable than native enzyme
D75N
-
mutation of an active site residue contributed by the other monomer in the active dimer
K72A
-
inactive active site mutant
K82A
-
crystallization data
Q185A
-
active site mutant, orotate recognition mutant
Q185A
-
220fold decrease in catalytic efficiency
Q185A/R203A
-
loss of activity
R160A
-
43fold decrease in catalytic efficiency
R160A/R203A
-
loss of activity
R160A/V182A
-
1700fold decrease in catalytic efficiency
R160A/Y206F
-
crystallization data, 340fold 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
Methanothermobacter thermautotrophicus DSM 1053
-
220fold decrease in catalytic efficiency
-
R160A
Methanothermobacter thermautotrophicus DSM 1053
-
43fold decrease in catalytic efficiency
-
R203A
Methanothermobacter thermautotrophicus DSM 1053
-
1900fold decrease in catalytic efficiency
-
T159A
Methanothermobacter thermautotrophicus DSM 1053
-
crystallization data
-
Y206F
Methanothermobacter thermautotrophicus DSM 1053
-
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
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
D37A
-
300fold reduced kcat/Km value
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
D96A/C155S
-
inactive mutant protein
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
-
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/R235A
-
less than 0.1% of wild-type activity
Q215A/Y217F
-
less than 0.1% of wild-type activity
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
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
S154A
-
mutant, effect of the mutation of the kinetic parameters for decarboxylation is determined
S154A/Q215A
-
mutant, effect of the mutation of the kinetic parameters for decarboxylation is determined
T100A
-
60fold reduced kcat/Km value
Y217A
-
active site mutant with increased dissociation constants for various ligands
Y217F
-
1.6% of wild-type activity
Y217F/R235A
-
less than 0.1% of wild-type activity
L123S
Methanobacterium thermoautotrophicus
-
8% of wild-type activity
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
L123N
Methanobacterium thermoautotrophicus DSM 1053
-
10% of wild-type activity
-
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
-
K93C
Saccharomyces cerevisiae BJ5424
-
absence of Zn2+ in mutant ODCase
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
human UMP synthase enzyme may be a potential cancer drug target
molecular biology
Q2HZ31
usage of the gene as a selection marker
medicine
-
orotidine 5-monophosphate decarboxylase of Plasmodium falciparum could be a target for the development of antimalarial drugs
biotechnology
B3GF12
to develop a marker recycling system, the orotidine-5'-monophosphate decarboxylase gene of Rhodosporidium toruloides is isolated