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Information on EC 4.1.1.23 - orotidine-5'-phosphate decarboxylase and Organism(s) Methanothermobacter thermautotrophicus and UniProt Accession O26232
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4.1.1.23 orotidine-5'-phosphate decarboxylaseIUBMB Comments
The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
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Word Map
- 4.1.1.23
- pyrimidine
-
phosphoribosyltransferase
- uracil
-
auxotrophic
- dihydroorotase
-
5-fluoroorotic
-
2.4.2.10
-
phosphoribosyl
- 6-azauridine
- pyrazofurin
-
transcarbamoylase
-
carbanions
- oprtase
-
aciduria
- 5-fluorouridine
- dianion
-
prototrophy
-
barbituric
-
succinate-grown
- phosphite
-
phosphodianion
-
pyre
- molecular biology
- pharmacology
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Methanothermobacter thermautotrophicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
odcase, ump synthase, orotidine 5'-monophosphate decarboxylase, orotidine-5'-phosphate decarboxylase, omp decarboxylase, orotidine-5'-monophosphate decarboxylase, ompdc, orotidine monophosphate decarboxylase, orotidylate decarboxylase, orotidine 5'-phosphate decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Orotidine 5'-monophosphate decarboxylase
-
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
-
-
-
-
ODCase
-
-
-
-
ODCase
-
-
OMPDCase
-
-
-
-
Orotidine 5'-monophosphate decarboxylase
-
-
-
-
Orotidine 5'-monophosphate decarboxylase
-
-
Orotidine monophosphate decarboxylase
-
-
-
-
Orotidine-5'-monophosphate decarboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
orotidine 5'-phosphate = UMP + CO2
catalytic mechanism
-
orotidine 5'-phosphate = UMP + CO2
mechanism, thermodynamic data
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
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 .
CAS REGISTRY NUMBER
COMMENTARY
9024-62-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyorotidine 5'-phosphate
2'-deoxyuridine 5'-phosphate + CO2
-
decreased catalytic rate compared with orotidine 5'-phosphate as substrate
-
?
4-Thioorotidine 5'-phosphate
4-Thiouridine 5'-phosphate + CO2
-
50% reduced kcat-value compared with orotidine 5'-phosphate as substrate
-
?
6-cyano-UMP + H2O
barbiturate ribonucleoside 5'-monophosphate + CN-
-
-
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
-
-
-
?
6-cyanouridine 5'-monophosphate
6-hydroxyuridine 5'-monophosphate + CN-
pseudohydrolysis process
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
the remote 5'-phosphate group of the substrate activates the enzyme 240 millionfold, the activation corresponds to an intrinsic binding energy of 11.4 kcal/mol. This intrinsic binding energy is used to allow interactions both near the N-terminus of the active site loop and across the domain interface that stabilize both the Ec-S and Ec-S* complexes relative to the Eo-S complex
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalytic mechanism, the remarkable catalytic power is almost exclusively achieved via ground state destabilization of the reactive part of substrate, which is compensated for by strong binding of the phosphate and ribose groups, and to a lesser extend via transition state stabilization, enzyme/active site structure, mode of substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism involving an equilibrium pre-protonation of orotidine 5'-phosphate C5 by the catalytic Lys-72 residue that greatly reduces the barrier to subsequent decarboxylation, Lys-72 is not critical for substrate binding
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, enzyme conformation is more distorted in the reactant state than in the transition state, the energy released from conformation relaxation provides the predominant contribution to the rate enhancement, the active site consists of a network of charged residues Lys-42, Asp-70, Lys-72, Asp-75b
-
?
Orotidine 5'-phosphate
UMP + CO2
-
mechanism, Lys-42, Asp-70, Lys-72 and Asp-75b form an alternate charged network around the reactive part of substrate, Lys-72 protonates the intermediate C6 carbanion
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the final step in the de novo biosynthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the last step of de novo pyrimidine synthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
last step in the biosynthesis of pyrimidine nucleotides
-
?
Orotidine 5'-phosphate
UMP + CO2
-
the enzyme catalyzes the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates, active site residues in ODCase are involved in an extensive hydrogen-bonding network, active site Lys42
-
-
?
additional information
?
-
-
not: 2-thioorotidine 5'-phosphate
-
?
additional information
?
-
-
the enzyme also converts 6-cyano-UMP to barbituric acid monophosphate with low activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Orotidine 5'-phosphate
UMP + CO2
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
-
-
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the final step in the de novo biosynthesis of UMP
-
?
Orotidine 5'-phosphate
UMP + CO2
-
catalyzes the last step of de novo pyrimidine synthesis
-
?
Orotidine 5'-phosphate
UMP + CO2
-
last step in the biosynthesis of pyrimidine nucleotides
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactors are involved in catalysis
-
additional information
-
ODCase contains no small molecule cofactors
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no metals are involved in catalysis
additional information
-
ODCase contains no metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-deoxy-2'-fluoro-6-iodo-beta-D-uridine 5'-O-monophosphate
-
-
2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl-cytosine
-
-
5-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
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-azido-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
-
6-cyano-1-methyluracil
-
modeling of binding and structure
6-cyano-2'-deoxy-2'-fluoro-beta-D-uridine 5'-O-monophosphate
-
reversible inhibitor
6-hydroxy-1-methyl uracil
-
modeling of binding and structure
6-hydroxyuridine 5'-monophosphate
-
tightly binding competitive inhibitor
barbiturate ribonucleoside 5'-monophosphate
-
very potent inhibitor
pyrazofurin-5'-monophosphate
-
slow tight binding inhibitor
additional information
-
inhibitor synthesis, overview
-
6-iodouridine 5'-monophosphate
-
irreversible inhibitor
6-iodouridine 5'-monophosphate
-
i.e. 6-iodo-UMP, irreversible inhibition, mass spectral analysis of the enzyme-inhibitor complex, binding to the enzyme is accompanied by loss of two protons and the iodo moiety, covalent bond formation
pyrazofurin
-
also known as pyrazomycin, potent inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
0.0055
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
0.024
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
0.03
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
0.033
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
0.1
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
0.1 - 1
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
0.13
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
0.3
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
0.6
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
0.7
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
0.98
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.9
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
0.0037
orotidine 5'-phosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics, most proficient enzyme known
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
0.56
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
1
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
1.1
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
1.1
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
1.4
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
1.5
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.5
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
2
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
2.3
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
3
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
4.1
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
5.3
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
additional information
additional information
-
50% reduced kcat-value for 4-thioorotidine 5'-phosphate compared with orotidine 5'-phosphate as substrate
-
additional information
additional information
-
highly proficient enzyme
-
additional information
additional information
-
remarkable catalytic power
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
orotidine 5'-phosphate
mutant T159V/V182A/Y206F, pH 7.1, 25°C
0.8
orotidine 5'-phosphate
mutant T159V/V182A, pH 7.1, 25°C
1.5
orotidine 5'-phosphate
mutant R203A, pH 7.1, 25°C
1.7
orotidine 5'-phosphate
mutant R160A/V182A, pH 7.1, 25°C
3.7
orotidine 5'-phosphate
mutant T159V/Y206F, pH 7.1, 25°C
8.5
orotidine 5'-phosphate
mutant R160A/Y206F, pH 7.1, 25°C
13
orotidine 5'-phosphate
mutant Q185A, pH 7.1, 25°C
15
orotidine 5'-phosphate
mutant V182A/Y206F, pH 7.1, 25°C
67
orotidine 5'-phosphate
mutant R160A, pH 7.1, 25°C
70
orotidine 5'-phosphate
mutant T159V, pH 7.1, 25°C
130
orotidine 5'-phosphate
mutant V182A, pH 7.1, 25°C
750
orotidine 5'-phosphate
mutant Y206F, pH 7.1, 25°C
2900
orotidine 5'-phosphate
wild-type, pH 7.1, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 55°C
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 55°C
0.00132
6-carbamoyl-UMP
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55°C
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 55°C
0.0286
6-cyanouridine
-
in 50 mM Tris, pH 7.5, 20 mM dithiothreitol, and 40 mM NaCl, at 55°C
0.0062
pyrazofurin-5'-monophosphate
-
in 50 mM Tris (pH 7.5), 20 mM dithiothreitol, and 40 mM NaCl, at 22°C
additional information
additional information
-
inhibition kinetics, isothermal calorimetry
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R160A/V182A
1700fold decrease in catalytic efficiency
R160A/Y206F
R203A
1900fold decrease in catalytic efficiency
T159V/V182A
3600fold decrease in catalytic efficiency
T159V/V182A/Y206F
20000fold decrease in catalytic efficiency
T159V/Y206F
780fold decrease in catalytic efficiency
V182A/Y206F
190fold decrease in catalytic efficiency
D70A
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
Q185A
-
active site mutant, orotate recognition mutant
S127A
-
active site mutant, orotate recognition mutant
R160A/Y206F
340fold decrease in catalytic efficiency
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Asp-70 makes a crucial contribution to enzyme stability
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, N.; Christendat, D.; Dharamsi, A.; Pai, E.F.
Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase
Acta Crystallogr. Sect. D
56
912-914
2000
Methanothermobacter thermautotrophicus
-
Wu, N.; Gillon, W.; Pai, E.F.
Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography
Biochemistry
41
4002-4011
2002
Methanothermobacter thermautotrophicus
Gao, J.
Catalysis by enzyme conformational change as illustrated by orotidine 5'-monophosphate decarboxylase
Curr. Opin. Struct. Biol.
13
184-192
2003
Methanothermobacter thermautotrophicus
Lee, T.S.; Chong, L.T.; Chodera, J.D.; Kollman, P.A.
An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase
J. Am. Chem. Soc.
123
12837-12848
2001
Methanothermobacter thermautotrophicus
Wu, N.; Mo, Y.; Gao, J.; Pai, E.F.
Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase
Proc. Natl. Acad. Sci. USA
97
2017-2022
2000
Methanothermobacter thermautotrophicus
Poduch, E.; Bello, A.M.; Tang, S.; Fujihashi, M.; Pai, E.F.; Kotra, L.P.
Design of inhibitors of orotidine monophosphate decarboxylase using bioisosteric replacement and determination of inhibition kinetics
J. Med. Chem.
49
4937-4945
2006
Methanothermobacter thermautotrophicus
Bello, A.M.; Poduch, E.; Fujihashi, M.; Amani, M.; Li, Y.; Crandall, I.; Hui, R.; Lee, P.I.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
A potent, covalent inhibitor of orotidine 5-monophosphate decarboxylase with antimalarial activity
J. Med. Chem.
50
915-921
2007
Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
Hu, H.; Boone, A.; Yang, W.
Mechanism of OMP decarboxylation in orotidine 5-monophosphate decarboxylase
J. Am. Chem. Soc.
130
14493-14503
2008
Methanothermobacter thermautotrophicus
Poduch, E.; Wei, L.; Pai, E.F.; Kotra, L.P.
Structural diversity and plasticity associated with nucleotides targeting orotidine monophosphate decarboxylase
J. Med. Chem.
51
432-438
2008
Homo sapiens, Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
Bello, A.M.; Poduch, E.; Liu, Y.; Wei, L.; Crandall, I.; Wang, X.; Dyanand, C.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
Structure-activity relationships of C6-uridine derivatives targeting plasmodia orotidine monophosphate decarboxylase
J. Med. Chem.
51
439-448
2008
Methanothermobacter thermautotrophicus, Plasmodium falciparum (Q8IJH3), Plasmodium falciparum
Chien, T.C.; Jen, C.H.; Wu, Y.J.; Liao, C.C.
Chemical models and their mechanistic implications for the transformation of 6-cyanouridine 5-monophosphate catalyzed by orotidine 5-monophosphate decarboxylase
Nucleic Acids Symp. Ser.
52
297-298
2008
Methanothermobacter thermautotrophicus (O26232)
Kotra, L.P.; Pai, E.F.
Inhibition of orotidine-5-monophosphate decarboxylase--discoveries and lessons
Nucleic Acids Symp. Ser.
52
85-86
2008
Helicobacter pylori, Homo sapiens, Staphylococcus aureus, Plasmodium falciparum, Methanothermobacter thermautotrophicus (O26232)
Meza-Avina, M.E.; Wei, L.; Liu, Y.; Poduch, E.; Bello, A.M.; Mishra, R.K.; Pai, E.F.; Kotra, L.P.
Structural determinants for the inhibitory ligands of orotidine-5'-monophosphate decarboxylase
Bioorg. Med. Chem.
18
4032-4041
2010
Saccharomyces cerevisiae, Helicobacter pylori, Homo sapiens, Methanothermobacter thermautotrophicus, Staphylococcus aureus, Plasmodium falciparum
Wu, Y.J.; Liao, C.C.; Jen, C.H.; Shih, Y.C.; Chien, T.C.
Chemical models and their mechanistic implications for the transformation of 6-cyanouridine 5-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase
Chem. Commun. (Camb. )
46
4821-4823
2010
Methanothermobacter thermautotrophicus
Lewis, M.; Meza-Avina, M.E.; Wei, L.; Crandall, I.E.; Bello, A.M.; Poduch, E.; Liu, Y.; Paige, C.J.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
Novel interactions of fluorinated nucleotide derivatives targeting orotidine 5'-monophosphate decarboxylase
J. Med. Chem.
54
2891-2901
2011
Homo sapiens, Methanothermobacter thermautotrophicus
Desai, B.J.; Wood, B.M.; Fedorov, A.A.; Fedorov, E.V.; Goryanova, B.; Amyes, T.L.; Richard, J.P.; Almo, S.C.; Gerlt, J.A.
Conformational changes in orotidine 5-monophosphate decarboxylase: a structure-based explanation for how the 5-phosphate group activates the enzyme
Biochemistry
51
8665-8678
2012
Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 1053 (O26232)
Fujihashi, M.; Ishida, T.; Kuroda, S.; Kotra, L.P.; Pai, E.F.; Miki, K.
Substrate distortion contributes to the catalysis of orotidine 5-monophosphate decarboxylase
J. Am. Chem. Soc.
135
17432-17443
2013
Methanothermobacter thermautotrophicus (O26232), Methanothermobacter thermautotrophicus DSM 1053 (O26232)
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