BRENDA - Enzyme Database show
show all sequences of 1.3.1.14

Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis

Argyrou, A.; Washabaugh, M.W.; Pickart, C.M.; Biochemistry 39, 10373-10384 (2000)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
activates
Faecalicatena orotica
cysteine
L-cysteine activates strongly, D-cysteine is also an activator, 1.8 mM L-cysteine is required at pH 8 for half-maximal activity, 10 mM for near-maximal activity
Faecalicatena orotica
dithiothreitol
activates
Faecalicatena orotica
glutathione
activates
Faecalicatena orotica
Mercaptoacetic acid
activates
Faecalicatena orotica
additional information
not activated by L-serine or L-alanine; thiol activation involves reduction of side chain of a cysteine residue corresponding to Cys-130, which functions as a general base
Faecalicatena orotica
Cloned(Commentary)
Commentary
Organism
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
Bacillus subtilis
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
Lactococcus lactis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.09
-
L-dihydroorotate
pH 8, 25°C
Faecalicatena orotica
0.13
-
NAD+
pH 8, 25°C
Faecalicatena orotica
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Bacillus subtilis
5829
-
cytosol
-
Enterococcus faecalis
5829
-
cytosol
-
Faecalicatena orotica
5829
-
cytosol
-
Lactococcus lactis
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
32000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
120000
-
analytical gel filtration
Faecalicatena orotica
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dihydroorotate + NAD+
Lactococcus lactis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Lactococcus lactis
r
dihydroorotate + NAD+
Enterococcus faecalis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Enterococcus faecalis
r
dihydroorotate + NAD+
Faecalicatena orotica
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Faecalicatena orotica
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Enterococcus faecalis
-
-
-
Faecalicatena orotica
-
identical with Clostridium oroticum
-
Lactococcus lactis
-
family IB enzyme, also contains family IA enzyme
-
Purification (Commentary)
Commentary
Organism
-
Faecalicatena orotica
Reaction
Reaction
Commentary
Organism
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
ping-pong steady-state kinetic mechanism
Enterococcus faecalis
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
ping-pong steady-state kinetic mechanism
Faecalicatena orotica
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
electron transfer mechanism
Lactococcus lactis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Faecalicatena orotica
Storage Stability
Storage Stability
Organism
-20°C, 0.27 M sodium phosphate, pH 6.3, over 6 months, less than 15% loss of activity
Faecalicatena orotica
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
equilibrium favours direction of orotate reduction
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
?
(S)-dihydroorotate + NAD+
equilibrium favours direction of orotate reduction
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
?
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Bacillus subtilis
orotate + NADH + H+
-
390568
Bacillus subtilis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Enterococcus faecalis
orotate + NADH + H+
-
390568
Enterococcus faecalis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Enterococcus faecalis
orotate + NADH + H+
-
390568
Enterococcus faecalis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
Subunits
Subunits
Commentary
Organism
heterotetramer
alpha2,beta2; alpha subunit is named PyrDB, beta subunit is named PyrK
Bacillus subtilis
heterotetramer
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
heterotetramer
alpha2,beta2, family IB enzyme; alpha subunit is named PyrDB, beta subunit is named PyrK
Lactococcus lactis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Faecalicatena orotica
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.97
-
Orotate
formation of L-dihydroorotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
Faecalicatena orotica
22
-
L-dihydroorotate
formation of orotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
Faecalicatena orotica
45
-
L-dihydroorotate
in presence of NAD+
Faecalicatena orotica
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.4
8.9
below and above the turnover number decreases
Faecalicatena orotica
Cofactor
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Bacillus subtilis
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Enterococcus faecalis
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Faecalicatena orotica
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer; iron-sulfur cluster resides on the beta subunit
Lactococcus lactis
FAD
two molecules FAD per heterotetramer
Bacillus subtilis
FAD
two molecules FAD per heterotetramer
Enterococcus faecalis
FAD
flavoprotein, ratio FAD to FMN 1:1; two molecules FAD per heterotetramer
Faecalicatena orotica
FAD
FAD is located on the beta subunit; two molecules FAD per heterotetramer
Lactococcus lactis
FMN
two molecules of FMN per heterotetramer
Bacillus subtilis
FMN
two molecules of FMN per heterotetramer
Enterococcus faecalis
FMN
flavoprotein, ratio FAD to FMN 1:1; two molecules of FMN per heterotetramer
Faecalicatena orotica
FMN
FMN is located on the alpha subunit; two molecules of FMN per heterotetramer
Lactococcus lactis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
activates
Faecalicatena orotica
cysteine
L-cysteine activates strongly, D-cysteine is also an activator, 1.8 mM L-cysteine is required at pH 8 for half-maximal activity, 10 mM for near-maximal activity
Faecalicatena orotica
dithiothreitol
activates
Faecalicatena orotica
glutathione
activates
Faecalicatena orotica
Mercaptoacetic acid
activates
Faecalicatena orotica
additional information
not activated by L-serine or L-alanine; thiol activation involves reduction of side chain of a cysteine residue corresponding to Cys-130, which functions as a general base
Faecalicatena orotica
Cloned(Commentary) (protein specific)
Commentary
Organism
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
Bacillus subtilis
genes encoding the two alpha and beta polypeptides, expression in Escherichia coli
Lactococcus lactis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Bacillus subtilis
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Enterococcus faecalis
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
Faecalicatena orotica
4Fe-4S-center
cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer; iron-sulfur cluster resides on the beta subunit
Lactococcus lactis
FAD
two molecules FAD per heterotetramer
Bacillus subtilis
FAD
two molecules FAD per heterotetramer
Enterococcus faecalis
FAD
flavoprotein, ratio FAD to FMN 1:1; two molecules FAD per heterotetramer
Faecalicatena orotica
FAD
FAD is located on the beta subunit; two molecules FAD per heterotetramer
Lactococcus lactis
FMN
two molecules of FMN per heterotetramer
Bacillus subtilis
FMN
two molecules of FMN per heterotetramer
Enterococcus faecalis
FMN
flavoprotein, ratio FAD to FMN 1:1; two molecules of FMN per heterotetramer
Faecalicatena orotica
FMN
FMN is located on the alpha subunit; two molecules of FMN per heterotetramer
Lactococcus lactis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.09
-
L-dihydroorotate
pH 8, 25°C
Faecalicatena orotica
0.13
-
NAD+
pH 8, 25°C
Faecalicatena orotica
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Bacillus subtilis
5829
-
cytosol
-
Enterococcus faecalis
5829
-
cytosol
-
Faecalicatena orotica
5829
-
cytosol
-
Lactococcus lactis
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
32000
-
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
120000
-
analytical gel filtration
Faecalicatena orotica
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dihydroorotate + NAD+
Lactococcus lactis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Lactococcus lactis
r
dihydroorotate + NAD+
Enterococcus faecalis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Enterococcus faecalis
r
dihydroorotate + NAD+
Faecalicatena orotica
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Faecalicatena orotica
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Faecalicatena orotica
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Faecalicatena orotica
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 0.27 M sodium phosphate, pH 6.3, over 6 months, less than 15% loss of activity
Faecalicatena orotica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
equilibrium favours direction of orotate reduction
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
?
(S)-dihydroorotate + NAD+
equilibrium favours direction of orotate reduction
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
?
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Bacillus subtilis
orotate + NADH + H+
-
390568
Bacillus subtilis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Enterococcus faecalis
orotate + NADH + H+
-
390568
Enterococcus faecalis
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
?
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Lactococcus lactis
orotate + NADH + H+
-
390568
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Enterococcus faecalis
orotate + NADH + H+
-
390568
Enterococcus faecalis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390568
Faecalicatena orotica
orotate + NADH + H+
-
390568
Faecalicatena orotica
r
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
alpha2,beta2; alpha subunit is named PyrDB, beta subunit is named PyrK
Bacillus subtilis
heterotetramer
alpha2,beta2, 2 * 32000 + 2 * 28000, SDS-PAGE
Faecalicatena orotica
heterotetramer
alpha2,beta2, family IB enzyme; alpha subunit is named PyrDB, beta subunit is named PyrK
Lactococcus lactis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Faecalicatena orotica
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.97
-
Orotate
formation of L-dihydroorotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
Faecalicatena orotica
22
-
L-dihydroorotate
formation of orotate, in absence of NAD+ or NADH, pH 8, 10 mM cysteine
Faecalicatena orotica
45
-
L-dihydroorotate
in presence of NAD+
Faecalicatena orotica
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.4
8.9
below and above the turnover number decreases
Faecalicatena orotica
Other publictions for EC 1.3.1.14
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)
701809
Kawasaki
b-Type dihydroorotate dehydrog ...
Bifidobacterium bifidum
Appl. Environ. Microbiol.
75
629-636
2009
-
-
-
-
-
-
4
-
-
-
1
-
-
4
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
674586
Combe
Lys-D48 is required for charge ...
Lactococcus lactis
J. Biol. Chem.
281
17977-17988
2006
-
-
-
-
4
-
-
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
3
-
-
-
-
-
-
3
-
4
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
654759
Mohsen
Thermodynamic basis of electro ...
Lactococcus lactis
Biochemistry
43
6498-6510
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390568
Argyrou
Dihydroorotate dehydrogenase f ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Biochemistry
39
10373-10384
2000
6
-
2
-
-
-
-
2
4
-
3
3
-
4
-
-
1
3
-
-
1
1
13
3
1
-
-
3
-
1
-
12
-
-
-
6
-
2
12
-
-
-
-
-
-
2
4
-
3
3
-
-
-
1
-
-
1
1
13
3
1
-
-
3
-
1
-
-
-
-
-
-
-
-
390569
Rowland
Structure of dihydroorotate de ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Structure
8
1227-1238
2000
-
5
-
1
-
-
-
-
4
-
-
3
-
4
-
-
1
1
-
-
-
-
11
3
-
-
-
-
-
-
-
12
-
-
-
-
5
-
12
1
-
-
-
-
-
-
4
-
-
3
-
-
-
1
-
-
-
-
11
3
-
-
-
-
-
-
-
-
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390928
Kahler
Biochemical characterization o ...
Bacillus subtilis, Mus musculus
Arch. Biochem. Biophys.
371
191-201
1999
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391244
Marcinkeviciene
Dihydroorotate dehydrogenase B ...
Enterococcus faecalis
Biochemistry
38
13129-13137
1999
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390917
Andersen
Two different dihydroorotate d ...
Lactococcus lactis
J. Bacteriol.
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3975-3982
1994
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390565
Buntain
-
Latent Inhibitors. Part 4. Irr ...
Faecalicatena orotica
J. Chem. Soc. Perkin Trans. I
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3175-3182
1988
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12
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390564
Friedmann
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Bestimmung mit Dihydroorotat-D ...
Faecalicatena orotica
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
2010-2014
1984
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390563
Blattmann
Stereospecificity of the dihyd ...
Faecalicatena orotica
Eur. J. Biochem.
30
130-137
1972
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390567
Nelson
Preparation of bovine xanthine ...
Faecalicatena orotica
J. Biol. Chem.
243
5368-5373
1968
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390566
Friedmann
Crystalline dihydroorotic dehy ...
Faecalicatena orotica
J. Biol. Chem.
235
1526-1530
1960
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390561
Friedmann
Purification and properties of ...
Faecalicatena orotica
J. Biol. Chem.
233
1398-1406
1958
3
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390562
Lieberman
Enzymic synthesis and breakdow ...
Faecalicatena orotica
Biochim. Biophys. Acta
12
223-234
1953
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