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Information on EC 1.5.1.34 - 6,7-dihydropteridine reductase and Organism(s) Homo sapiens and UniProt Accession P09417

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IUBMB Comments
The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P09417
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
BmDhpr, DHPR, dicDHPR, dihydropteridine reductase, dihydropteridine reductase (NADH), DQPR gene product, EC 1.6.99.10, EC 1.6.99.7, More, NADH-dihydropteridine reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydropteridine reductase
247
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dihydropteridine reductase (NADH)
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-
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DQPR gene product
247
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EC 1.6.99.7
247
formerly
NADH-dihydropteridine reductase
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NADPH-dihydropteridine reductase
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NADPH-specific dihydropteridine reductase
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reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide)
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additional information
247
enzyme is not identical with dihydrofolate reductase; NADPH-specific dihydropteridine reductase and NADH-dihydropteridine reductase have no common antigenic determinants, and show different physicochemical properties
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
show the reaction diagram
ordered bi-bi mechanism, binding of NADH first and dissociation of NAD+ last
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
70851-99-9
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9074-11-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
show the reaction diagram
-
-
-
r
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
show the reaction diagram
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-
-
-
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quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
show the reaction diagram
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
-
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quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
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-
-
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-
additional information
?
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essential part of the hydroxylating system of the aromatic amino acids phenylalanine, tyrosine and tryptophan, reduces quinonoid dihydropterine to regenerate tetrahydrobiopterin, main metabolic derangements caused by DHPR deficiency are hyperphenylalaninaemia and impaired production of the monoamine neurotransmitters dopamine, noradrenaline and serotonin, DHPR deficiency patients can develop severe and progressive neurological damage
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
show the reaction diagram
P09417
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-
-
r
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
P09417
last step of recycling of the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopteridine essential for aromatic amino acid hydroxylases and nitric oxide synthases, regulatory mechanism involve H2O2, enzyme inactivation because of H2O2 accumulation in the epidermis contributes to the pathomechanism of vitiligo
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-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
additional information
?
-
-
essential part of the hydroxylating system of the aromatic amino acids phenylalanine, tyrosine and tryptophan, reduces quinonoid dihydropterine to regenerate tetrahydrobiopterin, main metabolic derangements caused by DHPR deficiency are hyperphenylalaninaemia and impaired production of the monoamine neurotransmitters dopamine, noradrenaline and serotonin, DHPR deficiency patients can develop severe and progressive neurological damage
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminopterin
the DHFR inhibitor aminopterin inhibits tetrahydrobiopterin recycling. Aminopterin has no effect alone but slightly reduced L-citrulline formation and cGMP accumulation in the presence of dihydrobiopterin
(R)-2,10,11-trihydroxy-N-n-propylaporphine
-
0.0017 mM, 50% inhibition
(R)-2,10,11-trihydroxyaporphine
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0.0016 mM, 50% inhibition
(R)-2,11-dihydroxy-10-methoxy-aporphine
-
0.013 mM, 50% inhibition
(R)-apocodeine
-
0.079 mM, 50% inhibition
(R)-apomorphine
-
0.002 mM, 50% inhibition
(R)-N-chloroethylnorapomorphine
-
0.0029 mM, 50% inhibition
(R)-N-hydroxyethylnorapomorphine
-
0.001 mM, 50% inhibition
(R)-N-n-propylaporphine
-
-
(R)-N-n-propylnorapomorphine
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0.0018 mM, 50% inhibition
(R)-norapomorphine
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0.0028 mM, 50% inhibition
(S)-2,10,11-trihydroxyaporphine
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0.0015 mM, 50% inhibition
(S)-bulbocapnine
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0.148 mM, 50% inhibition
(S)-N-n-propylnorapomorphine
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0.0022 mM, 50% inhibition
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.0034 mM, 50% inhibition
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.0093 mM, 50% inhibition
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
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0.27 mM, 50% inhibition
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.003 mM, 50% inhibition
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
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0.3 mM, 50% inhibition
3',4'-deoxynorlaudanosolinecarboxylic acid
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noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
3(4-hydroxyphenyl)pyruvate
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0.0033 mM, 50% inhibition
3-iodotyrosine
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weak inhibition
3-O-methyldopamine
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0.06 mM, 50% inhibition
3-O-Methylepinephrine
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0.18 mM, 50% inhibition
3-phenylpyruvic acid
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4.7 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.0036 mM, 50% inhibition
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.0072 mM, 50% inhibition
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
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0.34 mM, 50% inhibition
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
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0.0059 mM, 50% inhibition
4-hydroxyphenyllactate
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0.058 mM, 50% inhibition
4-O-Methyldopamine
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0.069 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
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12 mM, 50% inhibition
5,5'-dithiobis(2-nitrobenzoate)
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0.1 mM, 60% inhibition
5-Hydroxydopamine
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0.042 mM, 50% inhibition
6-Hydroxydopamine
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0.029 mM, 50% inhibition
Adrenochrome
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alpha-Methyltyrosine
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1.1 mM, 50% inhibition
aminochrome
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oxidation product of adrenaline, competitive vs. NADH
aminopterin
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catecholamine
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cis-Diaminodichloroplatinum
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CoCl2
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0.01 mM, 30% inhibition
dopachrome
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0.6 mM, 50% inhibition
dopamine
epinephrine
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0.13 mM, 50% inhibition
H2O2
regulatory function in vivo, above 0.03 mM, oxidation of Met146 and Met151 leads to inactivation of the enzyme due to disruption of the NADH-binding site
HgCl2
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0.0001 mM, 60% inhibition
higenamine
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noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
higenamine-1-carboxylic acid
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noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
iodoacetamide
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K2PtCl4
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0.208 mM, half-life of inactivation: 3.1 min, NADH and 2 mM dithiothreitol completely protect
L-beta-3,4-dihydroxyphenylalanine
L-tyrosine
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; 0.44 mM, 50% inhibition
m-tyramine
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0.036 mM, 50% inhibition
N-ethylmaleimide
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1 mM, 76% inhibition
N-Methyldopamine
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0.027 mM, 50% inhibition
Noradrenalin
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no inhibition below 0.2 mM
norepinephrine
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0.2 mM, 50% inhibition
o-hydroxyphenylacetic acid
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6.9 mM, 50% inhibition
octopamine
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0.19 mM, 50% inhibition
p-chloromercuribenzoate
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0.01 mM, 70% inhibition
phenylacetic acid
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6.6 mM, 50% inhibition
phenylpyruvate
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salsolinol
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noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
tetrahydrobiopterin
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above 0.05 mM, substrate inhibition
trans-Diaminodichloroplatinum
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trans-Pt(NH3)Cl2
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1 mM, 96% inactivation after 2 h
tyramine
[4-hydroxyphenyl]acetic acid
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydro-pteridine
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37°C, pH 7.2
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
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0.017
5,6,7,8-tetrahydrobiopterin
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37°C, pH 7.2
0.366
6-methyl-quinonoid 7,8-(6H)-dihydropterin
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-
0.754
cis-6,7-dimethyl-quinonoid 7,8-(6H)-dihydropterin
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0.002 - 0.77
NADH
0.029 - 0.77
NADPH
0.018
quinonoid 2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
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recombinant enzyme
0.0008 - 0.0063
quinonoid 7,8-(6H)-dihydrobiopterin
0.669
quinonoid 7,8-(6H)-dihydropterin
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-
0.00015
quinonoid 7,8-dihydrobiopterin
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recombinant enzyme
0.0049 - 0.48
quinonoid-6-methyl-7,8-dihydropterin
0.0009 - 0.252
quinonoid-7,8-dihydrobiopterin
0.0009 - 0.144
quinonoid-7,8-dihydropterin
0.0011 - 0.017
tetrahydrobiopterin
additional information
additional information
MichaelisMenten kinetics of dihydrofolate reductase-catalyzed (6R)-5,6,7,8-tetrahydro-L-biopterin recycling
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
510
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
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17 - 280
NADH
20
NADPH
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recombinant enzyme
162
quinoid 2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
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recombinant enzyme
0.3 - 227
quinoid 6-methyl-7,8-dihydropterin
16.7 - 52.2
quinoid 7,8-dihydrobiopterin
15.7 - 51.2
quinoid 7,8-dihydropterin
10.9 - 113
quinonoid 7,8(6H)-dihydropterin
10.9 - 113
quinonoid 7,8-(6H)-dihydrobiopterin
200
tetrahydrobiopterin
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
(R)-2,10,11-trihydroxyapomorphine
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-
0.0022
(R)-apomorphine
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-
0.0022
(R)-N-n-propylaporphine
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-
0.0028
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
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noncompetitive inhibition
0.014 - 0.031
3',4'-deoxynorlaudanosoline-carboxylic acid
0.0037
3-(4-hydroxyphenyl)pyruvate
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-
0.024
6-Hydroxydopamine
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noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
0.0049
Adrenochrome
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-
0.01 - 0.011
aminopterin
0.006 - 0.014
dopamine
0.11 - 0.14
epinephrine
0.0015 - 0.0023
higenamine
0.0045
higenamine-1-carboxylic acid
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vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.26
L-Dopa
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-
0.25
L-tyrosine
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-
0.067
m-tyramine
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-
0.016 - 0.19
norepinephrine
0.01
phenylpyruvic acid
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uncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.09
salsolinol
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-
0.024 - 0.05
tyramine
0.074
[4-hydroxyphenyl]acetic acid
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
tyramine
Homo sapiens
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IC50: 0.04 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.706
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NADPH-specific liver enzyme
2.51
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20.2
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NADH-specific liver enzyme
56
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T119 insert mutant enzyme
224
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enzyme from brain
300
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W104G mutant enzyme
412
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recombinant enzyme
800
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recombinant enzyme
1180
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enzyme from brain
additional information
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0.003359 micromol reduced cytochrome c/min/5 mm disc, activity in blood of healty volunteers
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.6
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
inhibition of de novo biosynthesis of tetrahydrobiopterin by preincubating the cells for 24 h with the GTP cyclohydrolase inhibitor dihydroxyacetone phosphate (10 mM) diminishes L-citrulline formation. Addition of dihydrobiopterin fully restores L-citrulline formation. In addition to its effect on arginine-to-citrulline conversion, pretreatment of the cells with dihydroxyacetone phosphate reduces A23187-induced cGMP accumulation. Addition of tetrahydrobiopterin or dihydrobiopterin not only antagonizes the inhibitory effect of dihydroxyacetone phosphate but also increases cGMP accumulation. (6R)-5,6,7,8-Tetrahydro-L-biopterin availability regulates nitric oxide and superoxide formation by endothelial nitric oxide synthase (eNOS). At low tetrahydrobiopterin or low tetrahydrobiopterin to 7,8-dihydrobiopterin ratios the enzyme becomes uncoupled and generates superoxide at the expense of NO
physiological function
the enzyme catalyzes (6R)-5,6,7,8-tetrahydro-L-biopterin recycling in endothelial cytosols
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
DHPR_HUMAN
244
0
25790
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25774
-
2 * 25774, deduced from nucleotide sequence
26000
-
2 * 26000, SDS-PAGE
35000
-
2 * 35000, NADPH-specific liver enzyme, SDS-PAGE
47500
50000
54000
-
gradient PAGE
69000
-
NADPH-specific liver enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion, polyethylene glycol 4500, various concentrations of Tris phosphate buffer, pH 7.8, 8% methanol and 1 mM beta-mercaptoethanol, 2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G151S
-
mutation found in children suffering from phenylketonuria due to enzyme deficiency
G19D
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completely inactive
G23D
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mutation found in children suffering from phenylketonuria due to enzyme deficiency, inactive mutant enzyme
T119insert
-
reduced activity
W104G
-
similar activity as wild-type
Y150E
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150F
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150H
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150K
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150S
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
naphthoquinone affinity chromatography, 5'-AMP-Sepharose
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recombinant wild-type, G19D, W104G and T119insert mutant enzymes
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simple two step procedure i.e. affinity chromatography on Matrex gel blue A and hydrophobic chromatography on phenyl-Sepharose
-
wild-type and recombinant Y150H, Y150S, Y150F, Y150E, Y150K, G151S and G23D mutant enzymes
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloning of full-length cDNA, expression in COS cells
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expression of wild-type, G19D, W104G and T119insert mutant enzymes in Escherichia coli
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expression of wild-type, Y150H, Y150S, Y150F, Y150E, Y150K, G151S and G23D in Escherichia coli
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high-level expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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enzyme deficiency leads to progressive mental and physical retardation despite dietary phenylalanine restriction. Overview on genomic structure and location of natural mutations in the QDPR gene coding for enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Firgaira, F.A.; Cotton, R.G.H.; Jennings, I.; Danks, D.M.
Use of naphthoquinone adsorbent for the isolation of human dihydropteridine reductase
Methods Enzymol.
142
116-126
1987
Homo sapiens
Manually annotated by BRENDA team
Lockyer, J.; Cook, R.G.; Milstein, S.; Kaufman, S.; Woo, S.L.C.; Ledley, F.D.
Structure and expression of human dihydropteridine reductase
Proc. Natl. Acad. Sci. USA
84
3329-3333
1987
Homo sapiens, Ovis aries
Manually annotated by BRENDA team
Armarego, W.L.F.; Cotton, G.H.; Dahl, H.H.M.; Dixon, N.E.
High-level expression of human dihydropteridine reductase (EC 1.6.99.7), without N-terminal amino acid protection, in Escherichia coli
Biochem. J.
261
265-268
1989
Homo sapiens
Manually annotated by BRENDA team
Randles, D.
Temperature dependence of dihydropteridine reductase activity
Eur. J. Biochem.
155
301-304
1986
Homo sapiens
Manually annotated by BRENDA team
Firgaira, F.A.; Choo, K.H.; Cotton, R.G.H.; Danks, D.M.
Molecular and immunological comparison of human dihydropteridine reductase in liver, cultured fibroblasts and continuous lymphoid cells
Biochem. J.
197
45-53
1981
Homo sapiens
Manually annotated by BRENDA team
Armarego, W.L.F.; Waring, P.
Inhibition of human brain dihydropteridine reductase [E.C.1.6.99.10] by the oxidation products of catecholamines, the aminochromes
Biochem. Biophys. Res. Commun.
113
895-899
1983
Homo sapiens
Manually annotated by BRENDA team
Shen, R.S.
Potent inhibitory effects of tyrosine metabolites on dihydropteridine reductase from human and sheep liver
Biochim. Biophys. Acta
785
181-185
1984
Homo sapiens, Ovis aries, Rattus norvegicus
Manually annotated by BRENDA team
Abell, C.W.; Shen, R.S.; Gessner, W.; Brossi, A.
Inhibition of dihydropteridine reductase by novel 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs
Science
224
405-407
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shen, R.S.; Smith, R.V.; Davis, P.J.; Abell, C.W.
Inhibition of dihydropteridine reductase from human liver and rat striatal synaptosomes by apomorphine and its analogs
J. Biol. Chem.
259
8994-9000
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Armarego, W.L.F.; Ohnishi, A.; Taguchi, H.
New pteridine substrates for dihydropteridine reductase and horseradish peroxidase
Biochem. J.
234
335-342
1986
Homo sapiens
Manually annotated by BRENDA team
Shen, R.S.
Inhibition of dihydropteridine reductase by catecholamines and related compounds
Biochim. Biophys. Acta
743
129-135
1983
Homo sapiens
Manually annotated by BRENDA team
Armarego, W.L.F.; Ohnishi, A.
Inactivation of dihydropteridine reductase (human brain) by platinum(II) complexes
Eur. J. Biochem.
164
403-409
1987
Homo sapiens
Manually annotated by BRENDA team
Nakanishi, N.; Ozawa, K.; Yamada, S.
Determination of NADPH-specific dihydropteridine reductase in extract from human, monkey, and bovine livers by single radial immunodiffusion: selective assay differentiating NADPH- and NADH-specific enzymes
J. Biochem.
99
1311-1315
1986
Bos taurus, Homo sapiens, Macaca fascicularis
Manually annotated by BRENDA team
Waring, P.
The time-dependent inactivation of human brain dihydropteridine reductase by the oxidation products of L-dopa
Eur. J. Biochem.
155
305-310
1986
Homo sapiens
Manually annotated by BRENDA team
Shen, R.S.; Smith, R.V.; Davis, P.J.; Brubaker, A.; Abell, C.W.
Dopamine-derived tetrahydroisoquinolines. Novel inhibitors of dihydropteridine reductase
J. Biol. Chem.
257
7294-7297
1982
Homo sapiens
Manually annotated by BRENDA team
Nakanishi, N.; Hirayama, K.; Yamada, S.
A simple procedure for purification of NADH-specific dihydropteridine reductase from mammalian liver
J. Biochem.
92
1033-1040
1982
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Firgaira, F.A.; Cotton, G.H.; Danks, D.M.
Isolation and characterization of dihydropteridine reductase from human liver
Biochem. J.
197
31-43
1981
Homo sapiens
Manually annotated by BRENDA team
Craine, J.E.; Hall, E.S.; Kaufman, S.
The isolation and characterization of dihydropteridine reductase from sheep liver
J. Biol. Chem.
247
6082-6091
1972
Homo sapiens, Ovis aries, Rattus norvegicus
Manually annotated by BRENDA team
Nakanishi, N.; Hasegawa, H.; Yamada, S.; Akino, M.
Purification and physicochemical properties of NADPH-specific dihydropteridine reductase from bovine and human livers
J. Biochem.
99
635-644
1986
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Su, Y.; Varughese, K.I.; Xuong, N.H.; Bray, T.L.; Roche, D.J.; Whiteley, J.M.
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue
J. Biol. Chem.
268
26836-26841
1993
Homo sapiens
Manually annotated by BRENDA team
Varughese, K.I.; Xuong, N.H.; Whiteley, J.M.
Structural and mechanistic implications of incorporating naturally occurring aberrant mutations of human dihydropteridine reductase into a rat model
Int. J. Pept. Protein Res.
44
278-287
1994
Homo sapiens
Manually annotated by BRENDA team
Zhang, H.P.; Yang, N.; Armarego, W.L.F.
In vitro mutagenesis of human dihydropteridine reductase at the active site and at altered sites found in the reductases of deficient children
Pteridines
7
123-136
1996
Homo sapiens
-
Manually annotated by BRENDA team
Altindag, Z.; Sahin, G.
The change in dihydropteridin reductase activity in some diseases
Pharm. Sci.
2
335-337
1996
Homo sapiens
-
Manually annotated by BRENDA team
Hasse, S.; Gibbons, N.C.; Rokos, H.; Marles, L.K.; Schallreuter, K.U.
Perturbed 6-tetrahydrobiopterin recycling via decreased dihydropteridine reductase in vitiligo: more evidence for H2O2 stress
J. Invest. Dermatol.
122
307-313
2004
Homo sapiens, Homo sapiens (P09417)
Manually annotated by BRENDA team
Thoeny, B.; Blau, N.
Mutations in the BH4-metabolizing genes GTP cyclohydrolase I, 6-pyruvoyl-tetrahydropterin synthase, sepiapterin reductase, carbinolamine-4a-dehydratase, and dihydropteridine reductase
Hum. Mutat.
27
870-878
2006
Homo sapiens
Manually annotated by BRENDA team
Concolino, D.; Muzzi, G.; Rapsomaniki, M.; Moricca, M.T.; Pascale, M.G.; Strisciuglio, P.
Serum prolactin as a tool for the follow-up of treated DHPR-deficient patients
J. Inherit. Metab. Dis.
Suppl. 2
193-197
2008
Homo sapiens
Manually annotated by BRENDA team
Schmidt, K.; Kolesnik, B.; Gorren, A.; Werner, E.; Mayer, B.
Cell type-specific recycling of tetrahydrobiopterin by dihydrofolate reductase explains differential effects of 7,8-dihydrobiopterin on endothelial nitric oxide synthase uncoupling
Biochem. Pharmacol.
90
246-253
2014
Homo sapiens (P09417), Sus scrofa (Q8MJ30)
Manually annotated by BRENDA team
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