BRENDA - Enzyme Database
show all sequences of 1.3.1.2

Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase

Rosenbaum, K.; Schaffrath, B.; Hagen, W.R.; Jahnke, K.; Gonzalez, F.J.; Cook, P.F.; Schnackerz, K.D.; Protein Expr. Purif. 10, 185-191 (1997)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Sulfide
8.0 mol acid-labile sulfide per mol of subunit
Sus scrofa
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Sus scrofa
Inhibitors
Inhibitors
Commentary
Organism
Structure
5,6-dihydrouracil
-
Sus scrofa
ATP-ribose
dead-end inhibition
Sus scrofa
NADP+
competitive versus NADPH
Sus scrofa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
Uracil
-
Sus scrofa
0.006
-
NADPH
-
Sus scrofa
0.0066
-
NADPH
in presence of 2,6-dihydrouracil
Sus scrofa
0.023
-
Uracil
in presence of 2,6-dihydrouracil
Sus scrofa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
2 [4Fe-4S] clusters per subunit with 9.0 mol iron per mol of subunit
Sus scrofa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
107000
-
2 * 107000, SDS-PAGE
Sus scrofa
214000
-
recombinant from E. coli, native PAGE
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant protein
Sus scrofa
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
14
-
recombinant from Escherichia coli
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
uracil + NADPH
-
349228
Sus scrofa
5,6-dihydrouracil + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 107000, SDS-PAGE
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
flavin
contains 2 mol FMN and 2 mol FAD per mol of enzyme, tightly associated
Sus scrofa
NADPH
strictly dependent on
Sus scrofa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibitory reactions between uracil, NADP+ and dihydrouracil
Sus scrofa
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Sulfide
8.0 mol acid-labile sulfide per mol of subunit
Sus scrofa
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavin
contains 2 mol FMN and 2 mol FAD per mol of enzyme, tightly associated
Sus scrofa
NADPH
strictly dependent on
Sus scrofa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5,6-dihydrouracil
-
Sus scrofa
ATP-ribose
dead-end inhibition
Sus scrofa
NADP+
competitive versus NADPH
Sus scrofa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibitory reactions between uracil, NADP+ and dihydrouracil
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
Uracil
-
Sus scrofa
0.006
-
NADPH
-
Sus scrofa
0.0066
-
NADPH
in presence of 2,6-dihydrouracil
Sus scrofa
0.023
-
Uracil
in presence of 2,6-dihydrouracil
Sus scrofa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
2 [4Fe-4S] clusters per subunit with 9.0 mol iron per mol of subunit
Sus scrofa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
107000
-
2 * 107000, SDS-PAGE
Sus scrofa
214000
-
recombinant from E. coli, native PAGE
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein
Sus scrofa
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
14
-
recombinant from Escherichia coli
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
uracil + NADPH
-
349228
Sus scrofa
5,6-dihydrouracil + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 107000, SDS-PAGE
Sus scrofa
Other publictions for EC 1.3.1.2
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)
740810
Camadan
Purification and characterizat ...
Ovis aries
J. Enzyme Inhib. Med. Chem.
31
1335-1341
2016
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1
6
2
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1
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1
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1
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1
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1
1
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6
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1
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1
6
6
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2
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1
1
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1
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1
2
-
1
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1
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1
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1
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-
-
-
-
740412
Liu
Correlation between dihydropyr ...
Homo sapiens
Eur. Rev. Med. Pharmacol. Sci.
18
2772-2776
2014
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740288
Danielyan
Dependence of cell survival on ...
Homo sapiens
Cent. Nerv. Syst. Agents Med. Chem.
13
108-113
2013
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1
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1
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711309
Lohkamp
Insights into the mechanism of ...
Sus scrofa
Biochim. Biophys. Acta
1804
2198-2206
2010
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1
1
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7
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11
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1
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3
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1
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1
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1
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5
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5
2
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1
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7
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11
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1
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5
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1
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5
2
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2
2
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8
8
712566
Serve
Validation of an isocratic HPL ...
Homo sapiens
J. Chromatogr. B
878
1889-1892
2010
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1
1
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700526
Tsuchida
Expression of 5-fluorouracil-r ...
Homo sapiens
Oncol. Rep.
21
1037-1043
2009
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1
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689273
van Kuilenburg
Identification of two novel mu ...
Homo sapiens
Nucleosides Nucleotides Nucleic Acids
27
809-815
2008
-
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1
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2
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673121
Mattison
The uracil breath test in the ...
Homo sapiens
Clin. Cancer Res.
12
549-555
2006
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1
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670929
Di Paolo
Improved analysis of 5-Fluorou ...
Homo sapiens
Ther. Drug Monit.
27
362-368
2005
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1
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1
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1
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-
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-
672471
Van Kuilenburg
Identification of three novel ...
Homo sapiens, Sus scrofa
Biol. Chem.
386
319-324
2005
-
2
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1
5
-
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2
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5
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673116
Ogura
Dihydropyrimidine dehydrogenas ...
Homo sapiens
Clin. Cancer Res.
11
5104-5111
2005
-
1
-
-
2
-
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-
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1
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1
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1
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1
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1
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654897
Schnackerz
Dihydropyrimidine dehydrogenas ...
Bos taurus, Cupriavidus necator, Homo sapiens, Rattus norvegicus, Sus scrofa
Biochim. Biophys. Acta
1701
61-74
2004
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1
1
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4
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5
1
1
5
-
5
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5
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4
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10
1
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7
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1
7
1
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4
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5
1
1
5
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5
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4
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10
1
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349222
Balzarini
Lack of susceptibility of bicy ...
Homo sapiens, Mus musculus
Mol. Pharmacol.
61
1140-1145
2002
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2
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4
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2
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8
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4
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1
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8
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349233
Dobritzsch
Crystal structure of the produ ...
Sus scrofa
J. Biol. Chem.
277
13155-13166
2002
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1
1
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1
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1
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1
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1
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2
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349236
Van Kuilenburg
Novel disease-causing mutation ...
Homo sapiens
Biochem. J.
364
157-163
2002
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1
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656900
Mattison
A comparative analysis of tran ...
Mus musculus
Pharmacogenetics
12
133-144
2002
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677606
West
Pyrimidine base catabolism in ...
Pseudomonas putida
Antonie van Leeuwenhoek
80
163-167
2001
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1
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349232
Hagen
On the iron-sulfur clusters in ...
Sus scrofa
Eur. J. Biochem.
267
3640-3646
2000
1
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349226
Rosenbaum
Porcine Recombinant Dihydropyr ...
Sus scrofa
Biochemistry
37
17598-17609
1998
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1
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1
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1
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1
1
2
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1
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1
1
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2
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4
1
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2
1
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1
2
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1
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1
1
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1
1
2
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1
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2
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4
1
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-
349228
Rosenbaum
Purification, characterization ...
Sus scrofa
Protein Expr. Purif.
10
185-191
1997
1
-
1
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3
4
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1
2
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1
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1
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1
1
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1
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2
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1
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1
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1
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1
1
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349229
Van Kuilenburg
Subcellular localization of di ...
Rattus norvegicus
Biol. Chem.
378
1047-1053
1997
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1
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3
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1
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1
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1
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6
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1
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1
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6
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349142
Haaz
Impact of different fluorourac ...
Homo sapiens
Cancer Chemother. Pharmacol.
38
52-58
1996
2
1
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-
-
-
3
-
-
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1
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1
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5
-
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1
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2
1
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3
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1
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5
-
-
1
-
-
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-
-
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-
-
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349223
Schmitt
Purification and characterizat ...
Cupriavidus necator
Arch. Biochem. Biophys.
332
175-182
1996
1
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-
-
-
-
6
2
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1
2
1
-
1
-
-
1
1
-
-
1
1
6
1
1
-
-
-
-
-
-
3
4
-
-
1
-
-
3
-
-
-
-
6
4
2
-
1
2
1
-
-
-
1
-
-
1
1
6
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
349143
Milano
Inhibition of dihydropyrimidin ...
Homo sapiens
Cancer Chemother. Pharmacol.
34
147-152
1994
-
1
-
-
-
-
1
-
-
-
-
1
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1
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-
-
-
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5
5
-
1
-
1
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
5
5
-
1
-
1
-
-
-
-
-
-
-
-
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-
-
-
-
349224
Goudgaon
Phenylselenenyl- and phenylthi ...
Mus musculus
J. Med. Chem.
36
4250-4254
1993
-
-
-
-
-
-
2
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2
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-
-
-
-
1
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1
-
1
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1
2
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-
-
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-
1
-
-
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2
2
-
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-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
349227
Lu
Comparison of dihydropyrimidin ...
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
Biochem. Pharmacol.
46
945-952
1993
-
-
-
-
-
-
-
23
4
-
8
8
-
4
-
-
4
-
-
4
-
-
22
4
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
23
4
-
8
8
-
-
-
4
-
4
-
-
22
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
349234
Porter
Dihydropyrimidine dehydrogenas ...
Bos taurus
J. Biol. Chem.
268
19321-19327
1993
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-
-
-
-
-
2
5
-
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-
1
-
-
-
1
-
1
-
-
3
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
2
-
-
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-
2
-
5
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
349235
Podschun
Acid base catalytic mechanism ...
Sus scrofa
J. Biol. Chem.
268
3407-3413
1993
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1
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-
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2
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1
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1
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1
1
-
1
1
-
2
-
-
-
-
-
1
1
-
2
-
-
-
-
1
-
2
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
1
1
-
2
-
-
-
-
-
1
1
-
-
-
-
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-
-
349216
Porter
Mechanism-based inactivation o ...
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
J. Biol. Chem.
267
5236-5242
1992
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-
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4
32
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7
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
4
4
-
-
-
-
-
4
-
-
4
-
32
4
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
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-
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349220
Podschun
Stereochemistry of NADPH oxida ...
Sus scrofa
Biochem. Biophys. Res. Commun.
182
609-616
1992
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1
-
-
-
-
-
-
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1
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
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-
-
-
-
-
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349221
Porter
Inactivation of dihydropyrimid ...
Bos taurus
J. Biol. Chem.
266
19988-19994
1991
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-
-
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-
1
1
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2
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2
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-
-
1
1
-
5
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
1
-
-
-
-
-
2
-
-
-
-
-
1
1
-
5
-
1
-
-
-
-
-
-
-
-
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-
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-
349215
Klein
New high-performance liquid ch ...
Rattus norvegicus
J. Chromatogr.
529
431-436
1990
-
-
-
-
-
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1
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1
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-
-
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-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
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-
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-
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-
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-
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-
349219
Podschun
Kinetic mechanism of dihydropy ...
Sus scrofa
J. Biol. Chem.
265
12966-12972
1990
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-
-
-
-
-
3
2
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2
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1
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-
1
-
1
-
-
3
-
1
-
-
-
-
-
-
2
1
-
-
-
-
-
2
-
-
-
-
3
1
2
-
-
-
2
-
-
-
-
-
1
-
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
349213
Tuchman
Dihydropyrimidine dehydrogenas ...
Homo sapiens
Enzyme
42
15-24
1989
-
1
-
-
-
-
-
2
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3
-
1
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-
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2
1
-
4
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-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
-
-
-
-
-
2
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-
-
3
-
-
-
-
-
2
1
-
4
-
-
-
-
-
-
-
-
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349218
Podschun
Purification and characterizat ...
Sus scrofa
Eur. J. Biochem.
185
219-224
1989
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1
-
-
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1
1
2
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1
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1
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-
1
2
1
2
1
1
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
-
-
-
-
-
-
1
1
2
-
-
-
-
1
-
1
2
1
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
349225
Naguib
Structure-activity relationshi ...
Mus musculus
Biochem. Pharmacol.
38
1471-1480
1989
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-
-
-
-
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7
-
1
-
-
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-
3
-
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-
-
-
2
-
-
5
-
1
-
-
-
-
-
-
1
7
-
-
-
-
-
1
-
-
-
-
7
7
-
1
-
-
-
-
-
-
-
-
2
-
-
5
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
172058
Traut
Pyrimidine catabolism: individ ...
Rattus norvegicus
Biochemistry
23
2533-2539
1984
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
-
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-
1
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-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
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-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
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-
-
-
-
-
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349212
Shiotani
Purification and properties of ...
Rattus norvegicus
J. Biol. Chem.
256
219-224
1981
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-
-
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3
-
8
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1
2
2
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1
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-
1
-
-
1
7
-
10
1
1
-
1
-
1
-
-
3
-
-
-
-
-
-
3
-
-
3
-
-
-
8
-
1
2
2
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-
-
1
-
1
7
-
10
1
1
-
1
-
1
-
-
-
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349141
Hallock
Pyrimidine reducing enzymes of ...
Rattus norvegicus
Can. J. Biochem.
54
178-184
1976
-
-
-
-
-
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-
-
3
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1
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2
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1
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-
2
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5
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-
-
-
-
1
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
-
3
-
-
1
-
-
-
1
-
2
-
-
5
-
-
-
-
-
1
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349210
Fritzson
Properties and assay of dihydr ...
Rattus norvegicus
J. Biol. Chem.
235
719-725
1960
-
-
-
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4
1
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2
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2
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1
-
-
2
-
2
3
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
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-
-
-
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4
1
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-
2
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1
-
2
-
2
3
-
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-
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1
1
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-
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349211
Grisolia
The purification and propertie ...
Bos taurus
Biochim. Biophys. Acta
25
430-431
1957
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-
-
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-
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1
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1
2
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8
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-
1
-
-
2
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-
-
-
-
-
2
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-
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-
-
-
-
-
-
-
2
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-
1
-
1
2
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8
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-
-
-
-
1
-
-
-
-
-
-
-
-
-