BRENDA - Enzyme Database show
show all sequences of 1.5.1.34

NADPH-specific dihydropteridine reductase from bovine liver

Hasegawa, H.; Nakanishi, N.; Methods Enzymol. 142, 111-116 (1987)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
0.0001 mM, 50% inhibition
Bos taurus
aminopterin
1 mM, 50% inhibition, NADPH-specific enzyme
Bos taurus
L-tyrosine
noncompetitive vs. NADPH
Bos taurus
methopterin
0.7 mM, 50% inhibition of NADPH-specific enzyme
Bos taurus
NADP+
competitive vs. NADPH
Bos taurus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
NADPH
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
Bos taurus
0.0014
-
quinonoid 7,8-dihydro-6-methylpterin
cofactor NADPH, NADPH-specific enzyme
Bos taurus
0.0017
-
NADPH
reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme
Bos taurus
0.0068
-
quinonoid 7,8-dihydropterin
cofactor NADPH, NADPH-specific enzyme
Bos taurus
0.013
-
quinonoid 7,8-dihydro-6-methylpterin
cofactor NADH, NADPH-specific enzyme
Bos taurus
2.9
-
NADH
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
Bos taurus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
2 * 35000, NADPH-specific dihydropteridine reductase, SDS-PAGE
Bos taurus
65000
-
equilibrium centrifugation, NADPH-specific liver enzyme
Bos taurus
68000
-
NADPH-specific enzyme, gel filtration
Bos taurus
70000
-
NADPH-specific enzyme, native PAGE
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bos taurus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.972
-
NADPH-specific enzyme
Bos taurus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
-
484960
Bos taurus
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 35000, NADPH-specific dihydropteridine reductase, SDS-PAGE
Bos taurus
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
Bos taurus
NADPH
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
Bos taurus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0032
-
NADP+
NADPH-specific enzyme
Bos taurus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
Bos taurus
NADPH
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
Bos taurus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
0.0001 mM, 50% inhibition
Bos taurus
aminopterin
1 mM, 50% inhibition, NADPH-specific enzyme
Bos taurus
L-tyrosine
noncompetitive vs. NADPH
Bos taurus
methopterin
0.7 mM, 50% inhibition of NADPH-specific enzyme
Bos taurus
NADP+
competitive vs. NADPH
Bos taurus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0032
-
NADP+
NADPH-specific enzyme
Bos taurus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
NADPH
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
Bos taurus
0.0014
-
quinonoid 7,8-dihydro-6-methylpterin
cofactor NADPH, NADPH-specific enzyme
Bos taurus
0.0017
-
NADPH
reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme
Bos taurus
0.0068
-
quinonoid 7,8-dihydropterin
cofactor NADPH, NADPH-specific enzyme
Bos taurus
0.013
-
quinonoid 7,8-dihydro-6-methylpterin
cofactor NADH, NADPH-specific enzyme
Bos taurus
2.9
-
NADH
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
Bos taurus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
2 * 35000, NADPH-specific dihydropteridine reductase, SDS-PAGE
Bos taurus
65000
-
equilibrium centrifugation, NADPH-specific liver enzyme
Bos taurus
68000
-
NADPH-specific enzyme, gel filtration
Bos taurus
70000
-
NADPH-specific enzyme, native PAGE
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bos taurus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.972
-
NADPH-specific enzyme
Bos taurus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
-
484960
Bos taurus
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 35000, NADPH-specific dihydropteridine reductase, SDS-PAGE
Bos taurus
Other publictions for EC 1.5.1.34
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)
742313
Li
Molecular and enzymatic chara ...
Bombyx mori
Comp. Biochem. Physiol. B
186
20-27
2015
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1
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3
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5
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1
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2
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1
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1
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5
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3
1
1
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1
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1
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3
3
-
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741864
Schmidt
Cell type-specific recycling ...
Homo sapiens, Sus scrofa
Biochem. Pharmacol.
90
246-253
2014
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2
2
1
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2
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2
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2
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4
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2
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2
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2
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4
4
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724198
Gu
Regulation of transforming gro ...
Rattus norvegicus
Biochem. Cell Biol.
91
187-193
2013
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1
2
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1
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725004
Chen
Structural insights into the d ...
Dictyostelium discoideum
FEBS Lett.
585
2640-2646
2011
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5
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3
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712184
Manjarrez-Gutierrez
Dihydropteridine reductase act ...
Rattus norvegicus
Int. J. Dev. Neurosci.
28
621-624
2010
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701144
Lee
Diminished expression of dihyd ...
Rattus norvegicus
Proteomics
9
4851-4858
2009
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1
1
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686424
Perez-Reinado
The NprA nitroreductase requir ...
Rhodobacter capsulatus
Environ. Microbiol.
10
3174-3183
2008
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1
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1
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4
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3
1
1
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1
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688186
Concolino
Serum prolactin as a tool for ...
Homo sapiens
J. Inherit. Metab. Dis.
Suppl. 2
193-197
2008
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695339
Chen
Crystallization and preliminar ...
Dictyostelium discoideum
Acta Crystallogr. Sect. F
64
1013-1015
2008
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1
1
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1
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2
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668883
Thoeny
Mutations in the BH4-metaboliz ...
Homo sapiens
Hum. Mutat.
27
870-878
2006
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675692
Schormann
Crystal structure of Trypanoso ...
Trypanosoma cruzi
J. Struct. Biol.
152
64-75
2005
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655877
Wilquet
Dihydropteridine reductase as ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
J. Bacteriol.
186
351-355
2004
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1
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29
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6
1
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2
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6
1
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1
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656444
Hasse
Perturbed 6-tetrahydrobiopteri ...
Homo sapiens
J. Invest. Dermatol.
122
307-313
2004
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1
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654920
Wild
Physarum polycephalum expresse ...
Physarum polycephalum
Biol. Chem.
384
1057-1062
2003
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1
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6
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2
3
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10
1
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3
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10
1
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485009
Park
Molecular characterization of ...
Drosophila melanogaster
Biochim. Biophys. Acta
1492
247-251
2000
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485008
Chang
Comparative properties of thre ...
Rattus norvegicus
Adv. Exp. Med. Biol.
463
403-410
1999
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485007
Kiefer
The comparative interaction of ...
Rattus norvegicus
Biochemistry
36
9438-9445
1997
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5
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17
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2
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2
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13
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5
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17
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2
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13
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485004
Zhang
-
In vitro mutagenesis of human ...
Homo sapiens
Pteridines
7
123-136
1996
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1
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7
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33
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1
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1
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3
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21
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1
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7
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33
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1
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3
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21
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485005
Kiefer
Altered structural and mechani ...
Rattus norvegicus
J. Biol. Chem.
271
3437-3444
1996
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1
1
10
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19
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3
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1
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2
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9
1
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Varughese
Structural and mechanistic cha ...
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Armarego
High-level expression of human ...
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Vasudevan
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Kaufman
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Hasegawa
Dihydropteridine reductase fro ...
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1987
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NADPH-specific dihydropteridin ...
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Methods Enzymol.
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1987
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484961
Firgaira
Use of naphthoquinone adsorben ...
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1987
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484962
Scrimgeour
Dihydropteridine reductase fro ...
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1987
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Lockyer
Structure and expression of hu ...
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Shahbaz
Structural studies and isolati ...
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484968
Kwan
An enzyme immunoassay for the ...
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1987
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Armarego
Inactivation of dihydropteridi ...
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484969
Matthews
Preliminary x-ray diffraction ...
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Randles
Temperature dependence of dihy ...
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484983
Armarego
New pteridine substrates for d ...
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Biochem. J.
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1986
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484986
Nakanishi
Determination of NADPH-specifi ...
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The time-dependent inactivatio ...
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155
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1986
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Webber
Multiple forms of rat-liver di ...
Rattus norvegicus
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248
358-367
1986
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Nakanishi
Purification and physicochemic ...
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Nakanishi
Catalytic properties of NADPH- ...
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Randles
Reduced 6,6,8-trimethylpterins ...
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484979
Shen
Potent inhibitory effects of t ...
Homo sapiens, Ovis aries, Rattus norvegicus
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1984
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484980
Abell
Inhibition of dihydropteridine ...
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Science
224
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Inhibition of dihydropteridine ...
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484977
Bailey
6,6-Dimethylpterins: stable qu ...
Bos taurus, Ovis aries
Biochemistry
22
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1983
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Armarego
Inhibition of human brain dihy ...
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1
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4
1
1
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-
1
-
3
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
484984
Shen
Inhibition of dihydropteridine ...
Homo sapiens
Biochim. Biophys. Acta
743
129-135
1983
-
-
-
-
-
-
16
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
9
-
1
-
-
-
-
-
-
-
1
16
9
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484988
Shen
Dopamine-derived tetrahydroiso ...
Homo sapiens
J. Biol. Chem.
257
7294-7297
1982
-
-
-
-
-
-
7
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
7
11
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484989
Nakanishi
A simple procedure for purific ...
Bos taurus, Homo sapiens, Rattus norvegicus
J. Biochem.
92
1033-1040
1982
-
-
-
-
-
-
-
3
-
-
3
3
-
6
-
-
3
-
-
4
4
-
3
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
3
3
-
-
-
3
-
4
4
-
3
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
484973
Purdy
Inhibition of dihydropteridine ...
Rattus norvegicus
Biochem. J.
195
769-771
1981
-
-
-
-
-
-
1
2
-
-
-
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484975
Firgaira
Molecular and immunological co ...
Homo sapiens
Biochem. J.
197
45-53
1981
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
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-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484976
Webber
The effect of specific amino a ...
Rattus norvegicus
Arch. Biochem. Biophys.
206
145-152
1981
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484993
Firgaira
Isolation and characterization ...
Homo sapiens
Biochem. J.
197
31-43
1981
-
-
-
-
-
-
8
4
-
-
4
1
-
4
-
-
1
-
-
2
1
-
4
1
1
-
-
2
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
8
-
4
-
-
4
1
-
-
-
1
-
2
1
-
4
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
484974
Gould
Rat liver dihydropteridine red ...
Rattus norvegicus
Biochem. Soc. Trans.
8
565-566
1980
-
-
-
-
-
-
7
2
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
7
6
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484992
Hirayama
Dihydropteridine reductase and ...
Crithidia fasciculata
Biochim. Biophys. Acta
612
337-343
1980
-
-
-
-
-
2
2
2
-
-
1
-
-
2
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
-
2
-
2
-
2
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
484972
Webber
Pyridine nucleotide interactio ...
Rattus norvegicus
J. Biol. Chem.
253
6724-6729
1978
-
-
-
-
-
-
-
2
-
-
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-
-
3
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
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-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484971
Hasegawa
Dihydropteridine reductase fro ...
Bos taurus
J. Biochem.
81
169-177
1977
-
-
-
1
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484994
Nakanishi
A new enzyme, NADPH-dihydropte ...
Bos taurus
J. Biochem.
81
681-685
1977
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
1
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484963
Williams
Isolation and characterization ...
Pseudomonas sp.
J. Bacteriol.
127
1197-1207
1976
-
-
-
-
-
2
8
6
-
-
1
1
-
3
-
-
1
-
-
-
1
1
5
-
-
-
1
1
1
-
-
2
1
-
-
-
-
-
2
-
-
2
-
8
1
6
-
-
1
1
-
-
-
1
-
-
1
1
5
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
484995
Craine
The isolation and characteriza ...
Homo sapiens, Ovis aries, Rattus norvegicus
J. Biol. Chem.
247
6082-6091
1972
-
-
-
-
-
-
1
14
-
-
2
-
-
4
-
-
3
-
-
9
3
-
3
3
-
-
-
-
-
-
-
6
1
-
-
-
-
-
6
-
-
-
-
1
1
14
-
-
2
-
-
-
-
3
-
9
3
-
3
3
-
-
-
-
-
-
-
-
-
-
-
-
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-
484996
Lind
Dihydropteridine reductase. In ...
Rattus norvegicus
Eur. J. Biochem.
25
560-562
1972
-
-
-
-
-
-
6
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
5
-
-
-
-
-
-
-
-
2
4
-
-
-
-
-
2
-
-
-
-
6
4
-
-
-
-
-
-
-
-
1
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
484990
Musacchio
Beef adrenal medulla dihydropt ...
Bos taurus
Biochim. Biophys. Acta
191
485-487
1969
-
-
-
-
-
-
3
-
-
-
-
1
-
2
-
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-
-
-
2
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
484991
Nielsen
Dihydropteridine reductase. A ...
Bos taurus, Felis catus, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus
Eur. J. Biochem.
9
497-502
1969
-
-
-
-
-
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-
1
-
-
-
-
-
5
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
10
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
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-
-