BRENDA - Enzyme Database show
show all sequences of 1.3.98.1

Genetic diversity and kinetic properties of Trypanosoma cruzi dihydroorotate dehydrogenase isoforms

Sariego, I.; Annoura, T.; Nara, T.; Hashimoto, M.; Tsubouchi, A.; Iizumi, K.; Makiuchi, T.; Murata, E.; Kita, K.; Aoki, T.; Parasitol. Int. 55, 11-16 (2006)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
despite their genetic variations, kinetic properties of the three DHODs are conserved, these findings facilitate further exploitation of Trypanosoma cruzi DHOD inhibitors, as chemotherapeutic agents against Chagas' disease
Trypanosoma cruzi
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; genes subcloned int the EcoRI site of pUC18, PCR products cloned in vector pET100/D-TOPO, recombinant DHOD1 and DHOD2 expressed in Escherichia coli BL21-CodonPlus (DE3)-RP
Trypanosoma cruzi
Inhibitors
Inhibitors
Commentary
Organism
Structure
Orotate
competitively inhibits all three DHOD enzymes to a comparable level
Trypanosoma cruzi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0243
-
dihydroorotate
DHOD at 25°C
Trypanosoma cruzi
0.0259
-
dihydroorotate
native DHOD at 25°C
Trypanosoma cruzi
0.03
-
dihydroorotate
37°C, pH 7.0; 37°C, pH 7.0; DHOD1 and DHOD2 at 37°C
Trypanosoma cruzi
0.03
-
fumarate
37°C, pH 7.0; DHOD1 at 37°C
Trypanosoma cruzi
0.035
-
fumarate
37°C, pH 7.0; DHOD2 at 37°C
Trypanosoma cruzi
0.0439
-
fumarate
DHOD at 25°C
Trypanosoma cruzi
0.0534
-
fumarate
native DHOD at 25°C
Trypanosoma cruzi
0.067
-
fumarate
37°C, pH 7.0; DHOD3 at 37°C
Trypanosoma cruzi
0.071
-
dihydroorotate
37°C, pH 7.0; DHOD3 at 37°C
Trypanosoma cruzi
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34100
-
DHOD3, sequence analysis
Trypanosoma cruzi
34200
-
DHOD1 and DHOD2, sequence analysis
Trypanosoma cruzi
37000
-
recombinant DHOD1, DHOD2 and DHOD3 with an N-terminal His6-tag, affinity chromatography
Trypanosoma cruzi
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Trypanosoma cruzi
Q4D3W2
-
-
Trypanosoma cruzi
Q4DEJ0
-
-
Trypanosoma cruzi
Q4DGV2
-
-
Trypanosoma cruzi
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant DHOD1, DHOD2 and DHOD3 with an N-terminal His6-tag, by affinity chromatography
Trypanosoma cruzi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dihydroorotate + fumarate
-
676289
Trypanosoma cruzi
orotate + ?
-
-
-
?
dihydroorotate + fumarate
-
676289
Trypanosoma cruzi
orotate + reduced fumarate
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
DHOD1, DHOD2 and DHOD3
Trypanosoma cruzi
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0156
-
Orotate
inhibition of DHOD2 at 25°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0205
-
Orotate
inhibition of DHOD2 at 25°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0424
-
Orotate
37°C, pH 7.0, versus dihydroorotate; inhibition of DHOD3 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.049
-
Orotate
37°C, pH 7.0, versus fumarate; inhibition of DHOD3 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0573
-
Orotate
37°C, pH 7.0, versus dihydroorotate; inhibition of DHOD1 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0622
-
Orotate
37°C, pH 7.0, versus fumarate; inhibition of DHOD1 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0714
-
Orotate
37°C, pH 7.0, versus dihydroorotate; inhibition of DHOD2 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0773
-
Orotate
37°C, pH 7.0, versus fumarate; inhibition of DHOD2 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
Application (protein specific)
Application
Commentary
Organism
medicine
despite their genetic variations, kinetic properties of the three DHODs are conserved, these findings facilitate further exploitation of Trypanosoma cruzi DHOD inhibitors, as chemotherapeutic agents against Chagas' disease
Trypanosoma cruzi
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Trypanosoma cruzi
genes subcloned int the EcoRI site of pUC18, PCR products cloned in vector pET100/D-TOPO, recombinant DHOD1 and DHOD2 expressed in Escherichia coli BL21-CodonPlus (DE3)-RP
Trypanosoma cruzi
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Orotate
-
Trypanosoma cruzi
Orotate
competitively inhibits all three DHOD enzymes to a comparable level
Trypanosoma cruzi
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0156
-
Orotate
inhibition of DHOD2 at 25°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0205
-
Orotate
inhibition of DHOD2 at 25°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0424
-
Orotate
37°C, pH 7.0, versus dihydroorotate
Trypanosoma cruzi
0.0424
-
Orotate
inhibition of DHOD3 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.049
-
Orotate
37°C, pH 7.0, versus fumarate
Trypanosoma cruzi
0.049
-
Orotate
inhibition of DHOD3 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0573
-
Orotate
37°C, pH 7.0, versus dihydroorotate
Trypanosoma cruzi
0.0573
-
Orotate
inhibition of DHOD1 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0622
-
Orotate
37°C, pH 7.0, versus fumarate
Trypanosoma cruzi
0.0622
-
Orotate
inhibition of DHOD1 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
0.0714
-
Orotate
37°C, pH 7.0, versus dihydroorotate
Trypanosoma cruzi
0.0714
-
Orotate
inhibition of DHOD2 at 37°C, in the presence of 1 mM dihydroorotate
Trypanosoma cruzi
0.0773
-
Orotate
37°C, pH 7.0, versus fumarate
Trypanosoma cruzi
0.0773
-
Orotate
inhibition of DHOD2 at 37°C, in the presence of 1 mM fumarate
Trypanosoma cruzi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0243
-
dihydroorotate
DHOD at 25°C
Trypanosoma cruzi
0.0259
-
dihydroorotate
native DHOD at 25°C
Trypanosoma cruzi
0.03
-
dihydroorotate
37°C, pH 7.0
Trypanosoma cruzi
0.03
-
dihydroorotate
DHOD1 and DHOD2 at 37°C
Trypanosoma cruzi
0.03
-
fumarate
37°C, pH 7.0
Trypanosoma cruzi
0.03
-
fumarate
DHOD1 at 37°C
Trypanosoma cruzi
0.035
-
fumarate
37°C, pH 7.0
Trypanosoma cruzi
0.035
-
fumarate
DHOD2 at 37°C
Trypanosoma cruzi
0.0439
-
fumarate
DHOD at 25°C
Trypanosoma cruzi
0.0534
-
fumarate
native DHOD at 25°C
Trypanosoma cruzi
0.067
-
fumarate
37°C, pH 7.0
Trypanosoma cruzi
0.067
-
fumarate
DHOD3 at 37°C
Trypanosoma cruzi
0.071
-
dihydroorotate
37°C, pH 7.0
Trypanosoma cruzi
0.071
-
dihydroorotate
DHOD3 at 37°C
Trypanosoma cruzi
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34100
-
DHOD3, sequence analysis
Trypanosoma cruzi
34200
-
DHOD1 and DHOD2, sequence analysis
Trypanosoma cruzi
37000
-
recombinant DHOD1, DHOD2 and DHOD3 with an N-terminal His6-tag, affinity chromatography
Trypanosoma cruzi
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant DHOD1, DHOD2 and DHOD3 with an N-terminal His6-tag, by affinity chromatography
Trypanosoma cruzi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dihydroorotate + fumarate
-
676289
Trypanosoma cruzi
orotate + ?
-
-
-
?
dihydroorotate + fumarate
-
676289
Trypanosoma cruzi
orotate + reduced fumarate
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Trypanosoma cruzi
7
-
DHOD1, DHOD2 and DHOD3
Trypanosoma cruzi
Other publictions for EC 1.3.98.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740019
Reis
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724484
Cordeiro
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Biochimie
94
1739-1748
2012
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1
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723848
Liu
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Streptococcus mutans
Acta Crystallogr. Sect. F
67
182-187
2011
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724305
McDonald
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Lactococcus lactis
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50
2714-2716
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-
4
-
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1
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724890
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Saccharomyces cerevisiae
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10
1053-1061
2011
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1
1
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1
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725915
Ganesan
Yeast dihydroorotate dehydroge ...
Saccharomyces cerevisiae
Mol. Biochem. Parasitol.
177
29-34
2011
-
1
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5
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710846
Cheleski
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Trypanosoma cruzi
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399
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2010
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1
1
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4
1
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1
1
1
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711915
Cheleski
Novel insights for dihydroorot ...
Trypanosoma cruzi
Eur. J. Med. Chem.
45
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2010
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1
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11
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11
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700606
Pawlik
The effect of exon (19C>A) dih ...
Homo sapiens
Pharmacogenomics
10
303-309
2009
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684914
Pinheiro
Crystal structure of Trypanoso ...
Trypanosoma cruzi, Trypanosoma cruzi Y
Biochem. Biophys. Res. Commun.
369
812-817
2008
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689056
Arakaki
Characterization of Trypanosom ...
Trypanosoma brucei
Mol. Microbiol.
68
37-50
2008
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2
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696221
Inaoka
Structures of Trypanosoma cruz ...
Trypanosoma cruzi
Biochemistry
47
10881-10891
2008
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684848
Annoura
Dihydroorotate dehydrogenase a ...
Neobodo saliens
Biochem. Biophys. Res. Commun.
358
253-258
2007
-
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2
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1
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1
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1
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2
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685146
Fagan
Mechanism of flavin reduction ...
Lactococcus lactis
Biochemistry
46
4028-4036
2007
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1
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2
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2
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1
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1
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685158
Wolfe
Interaction of benzoate pyrimi ...
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Biochemistry
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Zameitat
Dihydroorotate dehydrogenase f ...
Saccharomyces cerevisiae
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Hurt
Structure of Plasmodium falcip ...
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Acta Crystallogr. Sect. D
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2006
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671092
Cordeiro
Crystallization and preliminar ...
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Acta Crystallogr. Sect. F
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676289
Sariego
Genetic diversity and kinetic ...
Trypanosoma cruzi
Parasitol. Int.
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Shi
Single-molecule kinetics revea ...
Lactococcus lactis
Proc. Natl. Acad. Sci. USA
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2006
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Feliciano
Cloning, expression, purificat ...
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High-throughput screening for ...
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656891
Nara
Inhibitory action of marine al ...
Trypanosoma cruzi
Parasitol. Int.
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2005
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Inaoka
Expression, purification and c ...
Trypanosoma cruzi
Acta Crystallogr. Sect. F
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875-878
2005
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675478
Annoura
The origin of dihydroorotate d ...
Euglena gracilis, Neobodo saliens, Parabodo caudatus, Trypanosoma cruzi
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113-127
2005
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Loffler
Dihydroorotate dehydrogenase m ...
Mus musculus
Nucleosides Nucleotides Nucleic Acids
23
1281-1285
2004
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Sierra Pagan
Cloning and expression of the ...
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Biochim. Biophys. Acta
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2003
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Norager
Lactococcus lactis dihydroorot ...
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2003
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Sorensen
A new type of dihydroorotate d ...
Saccharolobus solfataricus
Extremophiles
6
245-251
2002
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Haque
Parallel synthesis of potent, ...
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Takashima
Characterization of the dihydr ...
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2002
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657291
Ottosen
The dimeric dihydroorotate deh ...
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2002
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657355
Norager
E. coli dihydroorotate dehydro ...
Escherichia coli
Structure
10
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2002
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Vorisek
Enzymatic activities of Ura2 a ...
Saccharomyces cerevisiae
Yeast
19
449-457
2002
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Dihydrooxonate is a substrate ...
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Arch. Biochem. Biophys.
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286-294
2001
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Jordan
Catalytic properties of dihydr ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
378
84-92
2000
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390915
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The crystal structure of Lacto ...
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Protein Sci.
7
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Purification and characterizat ...
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Protein Sci.
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390912
Pascal
Mechanistic studies with deute ...
Crithidia fasciculata
Biochemistry
23
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1984
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Pascal
Purification and properties of ...
Crithidia fasciculata, Trypanosoma brucei brucei, Trypanosoma brucei brucei EATRO 110
Biochemistry
22
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Forman
Purification of the primary di ...
Rattus norvegicus
Prep. Biochem.
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1977
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Taylor
Biosynthetic dihydroorotate de ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Bacteriol.
119
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1974
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Biosynthetic dihydroorotate de ...
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Two functionally different dih ...
Pseudomonas sp.
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