Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(6R)-L-erythro-dihydrobiopterin + NADH + H+
?
-
-
-
?
(6R)-tetrahydrobiopterin + NAD(P)+
?
-
-
-
r
(6R,S)-6-hydroxy-methyltetrahydropterin + NAD(P)+
?
low activity
-
-
r
(6R,S)-6-methyl-tetrahydropterin + NAD(P)+
?
low activity
-
-
r
(6R,S)-tetrahydrodictyopterin + NAD(P)+
?
-
-
-
r
(6R,S)-tetrahydrofolic acid + NAD(P)+
?
low activity
-
-
r
(6R,S)-tetrahydroneopterin + NAD(P)+
?
low activity
-
-
r
(6S)-tetrahydrobiopterin + NAD(P)+
?
low activity
-
-
r
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
2-amino-4-hydroxy-6-methyl-5,6,7,8-tetrahydropteridine + NADH
?
-
-
-
-
?
2-amino-4-hydroxy-6-methyl-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6-methyl-tetrahydropteridine + NAD(P)+
-
-
-
?
2-amino-4-hydroxy-7-methyl-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-7-methyl-tetrahydropteridine + NAD(P)+
-
-
-
?
5,6,7,8-tetrahydrobiopterin + NAD+
quinonoid dihydrobiopterin + NADH + H+
-
-
-
-
r
5,6,7,8-tetrahydropteridine + NAD(P)+
6,7-dihydropteridine + NAD(P)H
enzyme is required for recycling of 6,7-dihydropteridine, in vivo regulation is related to growth phase
-
-
r
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD+
6,7-dimethyl-7,8-dihydropterin + NADH + H+
-
-
-
-
r
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD+
quinonoid 6,7-dimethyl dihydropteridine + NADH + H+
-
-
-
-
r
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
-
-
-
-
r
6,7-dimethyl-7,8-dihydropteridine + NADH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD+
-
NADH is preferred in vitro compared to NADPH
-
-
?
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
6,7-dimethyl-tetrahydropterin + NAD(P)+
?
low activity
-
-
r
6,7-dimethyldihydropterin + NADH + H+
6,7-dimethyltetrahydropterin + NAD+
-
-
-
?
6-methyl-dihydropterin + NADH + H+
6-methyl-tetrahydropterin + NAD+
-
-
-
-
r
6-methyldihydropterin + NADH + H+
quinoid 6,6-dimethyldihydropterin + NAD+
-
-
-
-
r
a 6,7-dihydropteridine + NAD(P)H + H+
a 5,6,7,8-tetrahydropteridine + NAD(P)+
-
-
-
-
?
a 6,7-dihydropteridine + NADPH + H+
a 5,6,7,8-tetrahydropteridine + NADP+
-
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
dihydrofolate + NADPH
tetrahydrofolate + NADP+
dihydropteroic acid + NAD(P)H
tetrahydropteroate + NAD(P)+
-
-
-
?
dihydropteroylglutamic acid + NAD(P)H
tetrahydropteroylglutamate + NAD(P)+
-
-
-
?
K3Fe(CN)6 + NAD(P)H
K4Fe(CN)6 + NAD(P)+
-
-
-
?
L-threo-neopterin + NAD+
?
-
-
-
-
r
quinoid 6-methyl-7,8-dihydropterin + NADH + H+
6-methyl-5,6,7,8-tetrahydropterin + NAD+
-
-
-
-
r
quinoid 7,8-(6H)-dihydropterin + NADH + H+
5,6,7,8-tetrahydropterin + NAD+
non-enzymatic reaction of quinoid 7,8-(6H)-dihydropterine to 7,8-dihydropterin
-
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
quinonoid (6R)-D-threo-dihydrobiopterin + NADH + H+
?
-
-
-
?
quinonoid 6,6-dimethyldihydropterin + NAD(P)H
6,6-dimethyltetrahydropterin + NAD(P)+
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
quinonoid 6,7-dimethyl-7,8-dihydropteridine + NADH + H+
6,7-dimethyl-5,6,7,8-tetrahydropteridine + NAD+
-
-
-
-
r
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
quinonoid 6-methyl-7,8-dihydropterin + NADH + H+
6-methyl-5,6,7,8-tetrahydropterin + NAD+
-
-
-
-
r
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
quinonoid 7,8-(6H)-dihydropterin + NADH + H+
5,6,7,8-tetrahydropterin + NAD+
-
-
-
-
r
quinonoid 7,8-(6H)-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
quinonoid 7,8-dihydropterin + NADH + H+
5,6,7,8-tetrahydropterin + NAD+
-
-
-
-
r
quinonoid 7,8-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
quinonoid dihydro-2-methylamino-4-hydroxy-6,7-dimethylpteridine + NAD(P)H
tetrahydro-2-methylamino-4-hydroxy-6,7-dimethylpteridine + NAD(P)+
-
approx. one-third of activity with 2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropterid
-
?
quinonoid dihydro-L-threo-neopterin + NAD(P)H
tetrahydro-L-threo-neopterin + NAD(P)+
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
r
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
quinonoid dihydromonapterin + NAD(P)H
tetrahydromonapterin + NAD(P)+
-
-
-
?
quinonoid dihydroneopterin + NAD(P)H
tetrahydroneopterin + NAD(P)+
-
-
-
?
quinonoid-6-methyl-7,8-dihydrobiopterin + NADH + H+
6-methyl-7,8-dihydropterin + NAD+
-
-
-
-
r
quinonoiddihydro-6-methylpterin + NADH + H+
?
-
-
-
-
r
additional information
?
-
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
-
-
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
NADH is 20fold more effective than NADPH
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
-
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
3% activity with NADPH
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
-
-
?
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
?
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
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
-
-
?
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
-
-
-
r
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
-
-
-
r
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
?
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
?
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
-
as the quinonoid forms of pterines are very unstable, the reaction is carried out with a dimethyl analogue in the presence of H2O2 and radish peroxidase to allow the continuous formation of 6,7-dimethyl-7,8-dihydropterine, activity is 25fold higher than the nitroreductase activity 2,4-dinitrophenol
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
-
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
-
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
-
pH 7.4, 37°C
-
-
?
dihydrofolate + NADPH
tetrahydrofolate + NADP+
-
-
-
-
?
dihydrofolate + NADPH
tetrahydrofolate + NADP+
-
-
-
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
-
-
-
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
-
NADH is 2.5fold more effective than NADPH
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
-
specific for NADH
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
-
-
-
-
?
quinonoid 6,6-dimethyldihydropterin + NAD(P)H
6,6-dimethyltetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,6-dimethyldihydropterin + NAD(P)H
6,6-dimethyltetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
enzyme from adrenal medulla
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
no activity with 6,6,8-trimethyl-7,8-(6H)-dihydropterin
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
NADPH-specific enzyme from liver, NADPH is 660times more effective than NADH
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
-
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
may also have an important role in regulation of catecholamine synthesis
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
more specific for NADH, 50% activity with NADPH, no activity with biopterin and 7,8-dihydrobiopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
enzyme also has pterin-independent NADH and NADPH oxidoreductase activity with potassium ferricyanide
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
enzyme prefers NADH
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
absolutely specific for quinonoid dihydro-isomer corresponding to 7,8-dihydropterins
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential component of the hepatic phenylalanine hydroxylating system
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
no marked specificity for the pteridine cofactor that occurs naturally in this organism L-threo-neopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential component of catecholamine biosynthetic metabolism
-
?
quinonoid 7,8-(6H)-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
r
quinonoid 7,8-(6H)-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
r
quinonoid 7,8-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
r
quinonoid 7,8-dihydropterin + NADPH + H+
5,6,7,8-tetrahydropterin + NADP+
-
-
-
-
r
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
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
-
-
?
additional information
?
-
substrate specificity, enzyme shows selectivity for pterin substrates with a 6-(1', 2'-dihydroxypropyl) substitution
-
-
?
additional information
?
-
-
substrate specificity, enzyme shows selectivity for pterin substrates with a 6-(1', 2'-dihydroxypropyl) substitution
-
-
?
additional information
?
-
-
in vivo role as dihydropteridine reductase involved in aromatic amino acids metabolism suggested
-
-
?
additional information
?
-
-
enzyme shows nitroreductase activity with several different substrates such as 2,4-dinitrophenol, 2,4-dinitrobenzoate and nitrofurazone
-
-
?
additional information
?
-
-
no activity with potassium ferricyanide, 6-biopterin, and 6-methyl-7,8-dihydropterine
-
-
?
additional information
?
-
-
no activity with potassium ferricyanide, 6-biopterin, and 6-methyl-7,8-dihydropterine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,6,7,8-tetrahydropteridine + NAD(P)+
6,7-dihydropteridine + NAD(P)H
enzyme is required for recycling of 6,7-dihydropteridine, in vivo regulation is related to growth phase
-
-
r
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
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
-
-
?
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
a 6,7-dihydropteridine + NAD(P)H + H+
a 5,6,7,8-tetrahydropteridine + NAD(P)+
-
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
-
pH 7.4, 37°C
-
-
?
quinoid 7,8-(6H)-dihydropterin + NADH + H+
5,6,7,8-tetrahydropterin + NAD+
non-enzymatic reaction of quinoid 7,8-(6H)-dihydropterine to 7,8-dihydropterin
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
-
-
-
?
additional information
?
-
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
-
-
-
r
6,7-dihydropteridine + NADPH + H+
5,6,7,8-tetrahydropteridine + NADP+
-
-
-
r
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
may also have an important role in regulation of catecholamine synthesis
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential component of the hepatic phenylalanine hydroxylating system
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
no marked specificity for the pteridine cofactor that occurs naturally in this organism L-threo-neopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
essential component of catecholamine biosynthetic metabolism
-
?
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
-
-
?
additional information
?
-
-
in vivo role as dihydropteridine reductase involved in aromatic amino acids metabolism suggested
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-2,10,11-trihydroxy-N-n-propylaporphine
(R)-2,10,11-trihydroxyaporphine
(R)-2,11-dihydroxy-10-methoxy-aporphine
(R)-N-chloroethylnorapomorphine
(R)-N-hydroxyethylnorapomorphine
(R)-N-n-propylnorapomorphine
(S)-2,10,11-trihydroxyaporphine
(S)-N-n-propylnorapomorphine
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
2,4-diaminopteroic acid
-
-
2,4-diaminopteroylglutamic acid
-
-
2,6-dichlorophenolindophenol
3',4'-deoxynorlaudanosolinecarboxylic acid
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
3(4-hydroxyphenyl)pyruvate
3-iodotyrosine
-
weak inhibition
3-O-methyldopamine
-
0.06 mM, 50% inhibition
3-O-Methylepinephrine
-
0.18 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
4-O-Methyldopamine
-
0.069 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
4-[(1R)-2-amino-1-hydroxyethyl]benzene-1,2-diol
5,5'-dithiobis(2-nitrobenzoate)
5-Hydroxydopamine
-
0.042 mM, 50% inhibition
6-Hydroxydopamine
-
0.029 mM, 50% inhibition
alpha-Methyltyrosine
-
1.1 mM, 50% inhibition
aminochrome
-
oxidation product of adrenaline, competitive vs. NADH
CdCl2
-
0.1 mM, complete inactivation
cis-Diaminodichloroplatinum
-
-
CoCl2
-
0.01 mM, 30% inhibition
dopachrome
-
0.6 mM, 50% inhibition
epinephrine
-
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
higenamine
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
higenamine-1-carboxylic acid
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
K2PtCl4
-
0.208 mM, half-life of inactivation: 3.1 min, NADH and 2 mM dithiothreitol completely protect
L-beta-3,4-dihydroxyphenylalanine
L-thyroxine
-
mixed-type inhibition
MgCl2
-
0.1 mM, complete inactivation
MnCl2
-
0.1 mM, complete inactivation
N-Methyldopamine
-
0.027 mM, 50% inhibition
NAD+
-
competitive vs. NADH
NADP+
-
competitive vs. NADPH
norepinephrine
-
0.2 mM, 50% inhibition
o-hydroxyphenylacetic acid
octopamine
-
0.19 mM, 50% inhibition
quinonoid 2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
quinonoid 6,6,8-trimethyl-7,8-dihydro(6H)pterin
-
0.2 mM, 50% inhibition
quiononoid 2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
salsolinol
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
tetrahydrobiopterin
-
above 0.05 mM, substrate inhibition
trans-Diaminodichloroplatinum
-
-
trans-Pt(NH3)Cl2
-
1 mM, 96% inactivation after 2 h
[4-hydroxyphenyl]acetic acid
-
-
(R)-2,10,11-trihydroxy-N-n-propylaporphine
-
0.0017 mM, 50% inhibition
(R)-2,10,11-trihydroxy-N-n-propylaporphine
-
0.0016 mM, 50% inhibition
(R)-2,10,11-trihydroxyaporphine
-
0.0016 mM, 50% inhibition
(R)-2,10,11-trihydroxyaporphine
-
0.0007 mM, 50% inhibition
(R)-2,11-dihydroxy-10-methoxy-aporphine
-
0.013 mM, 50% inhibition
(R)-2,11-dihydroxy-10-methoxy-aporphine
-
0.016 mM, 50% inhibition
(R)-apocodeine
-
0.079 mM, 50% inhibition
(R)-apocodeine
-
0.087 mM, 50% inhibition
(R)-apomorphine
-
0.002 mM, 50% inhibition
(R)-apomorphine
-
0.0012 mM, 50% inhibition
(R)-N-chloroethylnorapomorphine
-
0.0029 mM, 50% inhibition
(R)-N-chloroethylnorapomorphine
-
0.0029 mM, 50% inhibition
(R)-N-hydroxyethylnorapomorphine
-
0.001 mM, 50% inhibition
(R)-N-hydroxyethylnorapomorphine
-
0.0013 mM, 50% inhibition
(R)-N-n-propylaporphine
-
-
(R)-N-n-propylaporphine
-
-
(R)-N-n-propylnorapomorphine
-
0.0018 mM, 50% inhibition
(R)-N-n-propylnorapomorphine
-
0.0017 mM, 50% inhibition
(R)-norapomorphine
-
0.0028 mM, 50% inhibition
(R)-norapomorphine
-
0.0014 mM, 50% inhibition
(S)-2,10,11-trihydroxyaporphine
-
0.0015 mM, 50% inhibition
(S)-2,10,11-trihydroxyaporphine
-
0.0014 mM, 50% inhibition
(S)-bulbocapnine
-
0.148 mM, 50% inhibition
(S)-bulbocapnine
-
0.151 mM, 50% inhibition
(S)-N-n-propylnorapomorphine
-
0.0022 mM, 50% inhibition
(S)-N-n-propylnorapomorphine
-
0.0018 mM, 50% inhibition
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0034 mM, 50% inhibition
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0093 mM, 50% inhibition
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
0.27 mM, 50% inhibition
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.003 mM, 50% inhibition
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
0.3 mM, 50% inhibition
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
2,6-dichlorophenolindophenol
-
0.0001 mM, 50% inhibition
2,6-dichlorophenolindophenol
-
inhibition of NADPH-specific enzyme
3(4-hydroxyphenyl)pyruvate
-
0.0033 mM, 50% inhibition
3(4-hydroxyphenyl)pyruvate
-
0.0044 mM, 50% inhibition
3-phenylpyruvic acid
-
4.7 mM, 50% inhibition
3-phenylpyruvic acid
-
5.9 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0036 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0072 mM, 50% inhibition
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
0.34 mM, 50% inhibition
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0059 mM, 50% inhibition
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-hydroxyphenyllactate
-
0.058 mM, 50% inhibition
4-hydroxyphenyllactate
-
0.071 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
-
12 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
-
-
4-[(1R)-2-amino-1-hydroxyethyl]benzene-1,2-diol
-
no inhibition below 0.2 mM
4-[(1R)-2-amino-1-hydroxyethyl]benzene-1,2-diol
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
0.1 mM, 60% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
0.57 mM, 98% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
no inactivation in the presence of NADH
aminopterin
-
0.025 mM, 50% inhibition of NADH-specific enzyme, 1 mM, 50% inhibition of NADPH-specific enzyme
aminopterin
-
1 mM, 50% inhibition, NADPH-specific enzyme
aminopterin
-
no inhibition up to 0.1 mM
aminopterin
-
0.025 mM, 50% inhibition of NADH-specific enzyme, 1 mM, 50% inhibition of NADPH-specific enzyme
aminopterin
-
1 mM, 50% inhibition
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
aminopterin
-
competitive vs. 2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine
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
dopamine
-
no inhibition below 0.2 mM
dopamine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
dopamine
-
0.1 mM, 50% inhibition
HgCl2
-
0.0001 mM, 60% inhibition
HgCl2
-
0.002 mM, 50% inhibition, enzyme from brain
L-beta-3,4-dihydroxyphenylalanine
-
0.23 mM, 50% inhibition
L-beta-3,4-dihydroxyphenylalanine
-
0.02 mM, 50% inhibition
L-beta-3,4-dihydroxyphenylalanine
-
0.8 mM, 50% inhibition after 3 h, 80% inhibition after 16 h due to oxidation of L-DOPA to dopachrome which inhibits the enzyme
L-beta-3,4-dihydroxyphenylalanine
-
trivial name L-DOPA, 0.34 mM, 50% inhibition
L-tyrosine
-
noncompetitive vs. NADPH
L-tyrosine
-
0.44 mM, 50% inhibition
L-tyrosine
-
0.61 mM, 50% inhibition
m-tyramine
-
0.036 mM, 50% inhibition
m-tyramine
-
0.044 mM, 50% inhibition
methopterin
-
0.038 mM, 50% inhibition of NADH-specific enzyme
methopterin
-
0.7 mM, 50% inhibition of NADPH-specific enzyme
methopterin
-
0.038 mM, 50% inhibition of NADH-specific enzyme; 0.7 mM, 50% inhibition of NADPH-specific enzyme
methopterin
-
1 mM, 10% inhibition
methotrexate
-
no inhibition up to 0.1 mM
methotrexate
-
competitive vs. quinoid 6-methyl-7,8-dihydropterin
N-ethylmaleimide
-
1 mM, 76% inhibition
N-ethylmaleimide
-
5 mM, complete inhibition of reduced enzyme
o-hydroxyphenylacetic acid
-
6.9 mM, 50% inhibition
o-hydroxyphenylacetic acid
-
8.1 mM, 50% inhibition
p-chloromercuribenzoate
-
0.01 mM, 70% inhibition
p-chloromercuribenzoate
-
0.2 mM, 50% inhibition, enzyme from brain
p-chloromercuribenzoate
-
0.4 mM, 50% inhibition
p-chloromercuribenzoate
-
complete inactivation at inhibitor/enzyme ratios greater than 6/1, NADH protects
phenylacetic acid
-
6.6 mM, 50% inhibition
phenylacetic acid
-
6.9 mM, 50% inhibition
phenylpyruvate
-
-
tyramine
-
0.04 mM, 50% inhibition
tyramine
-
0.046 mM, 50% inhibition
additional information
-
enzyme from adrenal medulla, not inhibited by aminopterin and methotrexate
-
additional information
-
quinone products of L-DOPA oxidation are responsible for the time-dependent inactivation of the enzyme
-
additional information
-
not inhibited by EDTA, o-phenanthroline, and 2,2'-bipyridyl
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydro-pteridine
-
37°C, pH 7.2
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
-
-
0.34
2-Amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine
-
-
0.0152
2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
cofactor NADH
0.017 - 0.16
5,6,7,8-tetrahydrobiopterin
0.0063 - 0.0152
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
0.012 - 0.015
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.821
6,7-dimethyl-7,8-dihydropteridine
-
pH 7.4, 22°C, recombinant enzyme
0.03
6,7-dimethyldihydropterin
-
-
0.035
6-Methyl-dihydropterin
-
-
0.366
6-methyl-quinonoid 7,8-(6H)-dihydropterin
-
-
0.0014 - 0.013
6-methyl-tetrahydropterin
0.03
6-methyldihydropterin
-
-
0.754
cis-6,7-dimethyl-quinonoid 7,8-(6H)-dihydropterin
-
-
1.45
L-threo-neopterin
-
-
0.018
quinonoid 2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
-
recombinant enzyme
0.006 - 0.34
quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
0.4
Quinonoid 6,6-dimethyldihydropterin
0.008 - 0.46
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
0.0049 - 0.48
quinonoid 6-methyl-7,8-dihydropterin
0.0008 - 0.0063
quinonoid 7,8-(6H)-dihydrobiopterin
0.01 - 0.669
quinonoid 7,8-(6H)-dihydropterin
0.0014 - 0.013
quinonoid 7,8-dihydro-6-methylpterin
0.00015 - 0.0016
quinonoid 7,8-dihydrobiopterin
0.0009 - 0.144
quinonoid 7,8-dihydropterin
0.028
quinonoid dihydrobiobiopterin
-
K150E mutant enzyme
0.00032 - 1
quinonoid dihydrobiopterin
1.32
Quinonoid dihydromonapterin
-
-
1.05
Quinonoid dihydroneopterin
-
-
1.45
quinonoid L-threo-dihydroneopterin
-
-
0.525
quinonoid-6,7-dimethyl-7,8-dihydropterin
-
-
0.128
quinonoid-6-methyl-7,8-dihydrobiopterin
-
-
0.0009 - 0.252
quinonoid-7,8-dihydrobiopterin
0.0034
quinonoiddihydro-6-methylpterin
-
-
0.0009 - 0.017
tetrahydrobiopterin
additional information
additional information
-
0.017
5,6,7,8-tetrahydrobiopterin
-
37°C, pH 7.2
0.16
5,6,7,8-tetrahydrobiopterin
-
-
0.0063
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
cofactor NADPH
0.0152
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
cofactor NADH
0.012
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
-
0.015
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
-
0.0014
6-methyl-tetrahydropterin
-
NADPH-specific liver enzyme, cofactor NADPH
0.0056
6-methyl-tetrahydropterin
-
NADH-specific liver enzyme, cofactor NADH
0.0058
6-methyl-tetrahydropterin
-
NADH-specific liver enzyme, cofactor NADPH
0.013
6-methyl-tetrahydropterin
-
NADPH-specific liver enzyme, cofactor NADH
0.004
dihydrobiopterin
-
-
0.004
dihydrobiopterin
-
-
0.00079
NADH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin
0.00085
NADH
-
NADH-specific liver enzyme
0.0015
NADH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.0015
NADH
-
NADH-specific liver enzyme, substrate tetrahydrobiopterin
0.002
NADH
-
recombinant Y150S glutathione-S-transferase fusion mutant enzyme
0.002
NADH
-
recombinant Y150K glutathione-S-transferase fusion mutant enzyme
0.002
NADH
-
Y146F/A133S mutant enzyme
0.0024
NADH
-
recombinant Y150F mutant enzyme
0.003
NADH
-
Y146F mutant enzyme
0.0037
NADH
-
enzyme form III
0.004
NADH
-
reduction of quinonoid dihydrobiopterin
0.004
NADH
-
substrate tetrahydrobiopterin
0.0043
NADH
-
recombinant Y150H mutant enzyme
0.0044
NADH
-
recombinant Y150E glutathione-S-transferase fusion mutant enzyme
0.00441
NADH
-
enzyme form II
0.0049
NADH
-
recombinant Y150S mutant enzyme
0.005
NADH
-
recombinant Y150F glutathione-S-transferase fusion mutant enzyme
0.0055
NADH
-
enzyme form I
0.0057
NADH
-
reduction of quinonoid 2-amino-4-hydroxy-6,7-dimetyldihydropteridine
0.0057
NADH
-
substrate 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
0.0059
NADH
-
recombinant Y150H glutathione-S-transferase fusion mutant enzyme
0.0064
NADH
-
recombinant Y150E mutant enzyme
0.008
NADH
-
Y146H mutant enzyme
0.009
NADH
-
recombinant enzyme
0.01
NADH
-
Y146F mutant enzyme
0.0114
NADH
-
recombinant wild-type glutathione-S-transferase fusion enzyme
0.012
NADH
-
W86I mutant enzyme
0.013
NADH
-
recombinant wild-type enzyme
0.013
NADH
-
native liver enzyme
0.013
NADH
-
K150E mutant enzyme
0.017
NADH
-
A6V mutant enzyme
0.017
NADH
-
Y146H mutant enzyme
0.0172
NADH
-
recombinant wild-type enzyme
0.021
NADH
-
recombinant liver enzyme
0.021
NADH
-
K150I mutant enzyme
0.022
NADH
-
enzyme from brain
0.022
NADH
-
A133S mutant enzyme
0.025
NADH
-
A133S mutant enzyme
0.027
NADH
-
W104F mutant enzyme
0.027
NADH
-
Y146F/K150Q double mutant enzyme
0.029
NADH
-
K150Q mutant enzyme
0.0314
NADH
-
pH 7.4, 22°C, recombinant enzyme
0.036
NADH
-
D37I mutant enzyme
0.04651
NADH
apparent value, in 50 mM Tris-HCl, pH 7.5, at 25°C
0.074
NADH
-
NADH specific liver enzyme, substrate tetrahydrobiopterin
0.2
NADH
-
recombinant G23D mutant enzyme
0.276
NADH
-
recombinant G151S mutant enzyme
2.9
NADH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
2.9
NADH
-
NADPH specific liver enzyme, substrate 6-methyltetrahydropterin
0.0014
NADPH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
0.0014
NADPH
-
NADPH specific liver enzyme, substrate 6-methyl-tetrahydropterin
0.0017
NADPH
-
reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme
0.0017
NADPH
-
NADPH specific liver enzyme, substrate tetrahydrobiopterin
0.029
NADPH
-
37°C, pH 7.2
0.0709
NADPH
-
reduction of quinonoid dihydrobiopterin
0.0709
NADPH
-
substrate tetrahydrobiopterin
0.0729
NADPH
-
pH 7.4, 22°C, recombinant enzyme
0.074
NADPH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.076
NADPH
-
NADH-specific liver enzyme
0.08
NADPH
-
reduction of quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
0.0806
NADPH
-
substrate 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
0.095
NADPH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.095
NADPH
-
NADH specific liver enzyme, substrate 6-methyl-tetrahydropterin
0.135
NADPH
-
recombinant enzyme
0.006
quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
cofactor NADPH
0.34
quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
-
0.4
Quinonoid 6,6-dimethyldihydropterin
-
-
0.4
Quinonoid 6,6-dimethyldihydropterin
-
-
0.008
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
A133S mutant enzyme
-
0.027
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
recombinant wild-type enzyme
-
0.1
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
Y146F/A133S mutant enzyme
-
0.17
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
Y146H mutant enzyme
-
0.29
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
K150E mutant enzyme
-
0.46
quinonoid 6,7-dimethyl-7,8-dihydropteridine
-
Y146F mutant enzyme
-
0.0049
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant wild-type glutathione-S-transferase fusion enzyme
0.0062
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant G151S mutant enzyme
0.0181
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant wild-type enzyme
0.0819
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150H mutant enzyme
0.0874
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150H glutathione-S-transferase fusion mutant enzyme
0.0988
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant G23D mutant enzyme
0.149
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150E glutathione-S-transferase fusion mutant enzyme
0.165
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150F glutathione-S-transferase fusion mutant enzyme
0.283
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150S mutant enzyme
0.33
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150K glutathione-S-transferase fusion mutant enzyme
0.406
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150S glutathione-S-transferase fusion mutant enzyme
0.434
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150E mutant enzyme
0.48
quinonoid 6-methyl-7,8-dihydropterin
-
recombinant Y150F mutant enzyme
0.0008
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 20°C
0.0015
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 25°C
0.0024
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 30°C
0.0063
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 37°C
0.01
quinonoid 7,8-(6H)-dihydropterin
-
enzyme from brain
0.669
quinonoid 7,8-(6H)-dihydropterin
-
-
0.0014
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADPH, NADPH-specific enzyme
0.0056
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADH
0.0058
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADPH
0.013
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADH, NADPH-specific enzyme
0.00015
quinonoid 7,8-dihydrobiopterin
-
recombinant enzyme
0.0011
quinonoid 7,8-dihydrobiopterin
-
cofactor NADPH
0.0016
quinonoid 7,8-dihydrobiopterin
-
cofactor NADH
0.0009
quinonoid 7,8-dihydropterin
-
recombinant wild-type enzyme
0.0068
quinonoid 7,8-dihydropterin
-
cofactor NADPH, NADPH-specific enzyme
0.0075
quinonoid 7,8-dihydropterin
-
recombinant G151S mutant enzyme
0.144
quinonoid 7,8-dihydropterin
-
recombinant G23D mutant enzyme
0.00032
quinonoid dihydrobiopterin
-
-
0.0004
quinonoid dihydrobiopterin
-
recombinant wild-type enzyme
0.0004
quinonoid dihydrobiopterin
-
A133S mutant enzyme
0.0009
quinonoid dihydrobiopterin
-
Y146F mutant enzyme
0.001
quinonoid dihydrobiopterin
-
cofactor NADH
0.0025
quinonoid dihydrobiopterin
-
enzyme form III
0.0028
quinonoid dihydrobiopterin
-
enzyme form I
0.00285
quinonoid dihydrobiopterin
-
enzyme form II
0.007
quinonoid dihydrobiopterin
-
Y146H mutant enzyme
0.009
quinonoid dihydrobiopterin
-
cofactor NADPH
0.02
quinonoid dihydrobiopterin
-
A133S mutant enzyme
0.023
quinonoid dihydrobiopterin
-
Y146H mutant enzyme
0.024
quinonoid dihydrobiopterin
-
Y146F/A133S mutant enzyme
0.026
quinonoid dihydrobiopterin
-
K150I mutant enzyme
0.027
quinonoid dihydrobiopterin
-
recombinant wild-type enzyme
0.03
quinonoid dihydrobiopterin
-
D37I mutant enzyme
0.033
quinonoid dihydrobiopterin
-
K150Q mutant enzyme
0.039
quinonoid dihydrobiopterin
-
K150M mutant enzyme
0.041
quinonoid dihydrobiopterin
-
Y146F/K150Q double mutant enzyme
0.07
quinonoid dihydrobiopterin
-
W86I mutant enzyme
0.16
quinonoid dihydrobiopterin
-
-
0.226
quinonoid dihydrobiopterin
-
-
0.308
quinonoid dihydrobiopterin
-
Y146F mutant enzyme
1
quinonoid dihydrobiopterin
-
Y146F/K150E mutant enzyme, more than
0.0009
quinonoid-7,8-dihydrobiopterin
-
recombinant wild-type enzyme
0.004
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150H mutant enzyme
0.0305
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150S mutant enzyme
0.0593
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150F mutant enzyme
0.252
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150E mutant enzyme
0.0009
tetrahydrobiopterin
-
cofactor NADPH
0.001
tetrahydrobiopterin
-
cofactor NADH
0.0011
tetrahydrobiopterin
-
-
0.0011
tetrahydrobiopterin
-
-
0.0011
tetrahydrobiopterin
-
NADH-specific liver enzyme, cofactor NADPH
0.0016
tetrahydrobiopterin
-
NADH-specific liver enzyme, cofactor NADH
0.0068
tetrahydrobiopterin
-
NADPH-specific liver enzyme, cofactor NADPH
0.017
tetrahydrobiopterin
-
-
additional information
additional information
Michaelis-Menten kinetics of dihydrofolate reductase-catalyzed (6R)-5,6,7,8-tetrahydro-L-biopterin recycling, the enzyme shows high affinity for dihydrobiopterin
-
additional information
additional information
MichaelisMenten kinetics of dihydrofolate reductase-catalyzed (6R)-5,6,7,8-tetrahydro-L-biopterin recycling
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kaufman, S.
Dihydropteridine reductase from sheep liver
Methods Enzymol.
142
97-103
1987
Ovis aries
brenda
Hasegawa, H.; Nakanishi, N.
Dihydropteridine reductase from bovine liver
Methods Enzymol.
142
103-110
1987
Bos taurus
brenda
Hasegawa, H.; Nakanishi, N.
NADPH-specific dihydropteridine reductase from bovine liver
Methods Enzymol.
142
111-116
1987
Bos taurus
brenda
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
brenda
Scrimgeour, K.G.; Cheema-Dhadli, S.
Dihydropteridine reductase from sheep brain
Methods Enzymol.
142
127-132
1987
Ovis aries
brenda
Williams, C.D.; Dickens, G.; Letendre, C.H.; Guroff, G.; Haines, C.; Shiota, T.
Isolation and characterization of dihydropteridine reductase from Pseudomonas species
J. Bacteriol.
127
1197-1207
1976
Pseudomonas sp.
brenda
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
Ovis aries, Homo sapiens
brenda
Matthews, D.A.; Varughese, K.I.; Skinner, M.; Xuong, N.H.; Hoch, J.; Trach, K.; Schneider, M.; Bray, T.; Whiteley, J.M.
Role of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase
Arch. Biochem. Biophys.
287
234-239
1991
Rattus norvegicus
brenda
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
brenda
Shahbaz, M.; Hoch, J.A.; Trach, A.; Hural, J.A.; Webber, S.; Whiteley, J.M.
Structural studies and isolation of cDNA clones providing the complete sequence of rat liver dihydropteridine reductase
J. Biol. Chem.
262
16412-16416
1987
Rattus norvegicus
brenda
Kwan, S.W.; Shen, R.S.; Abell, C.W.
An enzyme immunoassay for the quantitation of dihydropteridine reductase
Anal. Biochem.
164
391-396
1987
Rattus norvegicus
brenda
Matthews, D.A.; Webber, S.; Whiteley, J.M.
Preliminary x-ray diffraction characterization of crystalline rat liver dihydropteridine reductase
J. Biol. Chem.
261
3891-3893
1986
Rattus norvegicus
brenda
Randles, D.
Temperature dependence of dihydropteridine reductase activity
Eur. J. Biochem.
155
301-304
1986
Homo sapiens
brenda
Hasegawa, H.
Dihydropteridine reductase from bovine liver. Purification, crystallization, and isolation of a binary complex with NADH
J. Biochem.
81
169-177
1977
Bos taurus
brenda
Webber, S.; Whiteley, J.M.
Pyridine nucleotide interaction with rat liver dihydropteridine reductase
J. Biol. Chem.
253
6724-6729
1978
Rattus norvegicus
brenda
Purdy, S.E.; Blair, J.A.; Barford, P.A.
Inhibition of dihydropteridine reductase by dopamine
Biochem. J.
195
769-771
1981
Rattus norvegicus
brenda
Gould, K.G.; Engel, P.C.
Rat liver dihydropteridine reductase inhibition
Biochem. Soc. Trans.
8
565-566
1980
Rattus norvegicus
brenda
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
brenda
Webber, S.; Whiteley, J.M.
The effect of specific amino acid modifications on the catalytic properties of rat liver dihydropteridine reductase
Arch. Biochem. Biophys.
206
145-152
1981
Rattus norvegicus
brenda
Bailey, S.W.; Ayling, J.E.
6,6-Dimethylpterins: stable quinoid dihydropterin substrate for dihydropteridine reductase and tetrahydropterin cofactor for phenylalanine hydroxylase
Biochemistry
22
1790-1798
1983
Bos taurus, Ovis aries
brenda
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
brenda
Shen, R.S.
Potent inhibitory effects of tyrosine metabolites on dihydropteridine reductase from human and sheep liver
Biochim. Biophys. Acta
785
181-185
1984
Ovis aries, Homo sapiens, Rattus norvegicus
brenda
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
brenda
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
brenda
Randles, D.; Armarego, L.F.
Reduced 6,6,8-trimethylpterins. Preparation, properties and enzymic reactivities with dihydropteridine reductase, phenylalanine hydroxylase and tyrosine hydroxylase
Eur. J. Biochem.
146
467-474
1985
Ovis aries
brenda
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
brenda
Shen, R.S.
Inhibition of dihydropteridine reductase by catecholamines and related compounds
Biochim. Biophys. Acta
743
129-135
1983
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Musacchio, J.M.
Beef adrenal medulla dihydropteridine reductase
Biochim. Biophys. Acta
191
485-487
1969
Bos taurus
brenda
Nielsen, K.H.; Simonsen, V.; Lind, K.E.
Dihydropteridine reductase. A method for the measurement of activity, and investigations of the specificity for NADH and NADPH
Eur. J. Biochem.
9
497-502
1969
Bos taurus, Oryctolagus cuniculus, Felis catus, Ovis aries, Rattus norvegicus
brenda
Hirayama, K.; Nakanisi, N.; Sueoka, T.; Katoh, S.; Yamada, S.
Dihydropteridine reductase and tetrahydropterin in Crithidia fasciculata cells
Biochim. Biophys. Acta
612
337-343
1980
Crithidia fasciculata
brenda
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
brenda
Nakanishi, N.; Hasegawa, H.; Watabe, S.
A new enzyme, NADPH-dihydropteridine reductase in bovine liver
J. Biochem.
81
681-685
1977
Bos taurus
brenda
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
Ovis aries, Homo sapiens, Rattus norvegicus
brenda
Lind, K.E.
Dihydropteridine reductase. Investigation of the specificity for quinoid dihydropteridine and the inhibition by 2,4-diaminopteridines
Eur. J. Biochem.
25
560-562
1972
Rattus norvegicus
brenda
Vasudevan, S.G.; Shaw, D.C.; Armarego, W.L.F.
Dihydropteridine reductase from Escherichia coli
Biochem. J.
255
581-588
1988
Escherichia coli
brenda
Webber, S.; Hural, J.A.; Whiteley, J.M.
Multiple forms of rat-liver dihydropteridine reductase identified by their differing isoelectric points
Arch. Biochem. Biophys.
248
358-367
1986
Rattus norvegicus
brenda
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
brenda
Nakanishi, N.; Hasegawa, H.; Akino, M.; Yamada, S.
Catalytic properties of NADPH-specific dihydropteridine reductase from bovine liver
J. Biochem.
99
645-652
1986
Bos taurus
brenda
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
brenda
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
brenda
Varughese, K.I.; Xuong, N.H.; Kiefer, P.M.; Matthews, D.A.; Whiteley, J.M.
Structural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases
Proc. Natl. Acad. Sci. USA
91
5582-5586
1994
Rattus norvegicus
brenda
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
-
brenda
Kiefer, P.M.; Varughese, K.I.; Su, Y.; Xuong, N.H.; Chang, C.F.; Gupta, P.; Bray, T.; Whiteley, J.M.
Altered structural and mechanistic properties of mutant dihydropteridine reductases
J. Biol. Chem.
271
3437-3444
1996
Rattus norvegicus
brenda
Altindag, Z.; Sahin, G.
The change in dihydropteridin reductase activity in some diseases
Pharm. Sci.
2
335-337
1996
Homo sapiens
-
brenda
Kiefer, P.M.; Grimshaw, C.E.; Whiteley, J.M.
The comparative interaction of quinonoid (6R)-Dihydrobiopterin and an alternative dihydropterin substrate with wild-type and mutant rat dihydropteridine reductases
Biochemistry
36
9438-9445
1997
Rattus norvegicus
brenda
Chang, C.F.; Bray, T.; Varughese, K.I.; Whiteley, J.M.
Comparative properties of three pteridine reductases
Adv. Exp. Med. Biol.
463
403-410
1999
Rattus norvegicus
brenda
Park, D.; Park, S.; Yim, J.
Molecular characterization of Drosophila melanogaster dihydropteridine reductase
Biochim. Biophys. Acta
1492
247-251
2000
Drosophila melanogaster
brenda
Wild, C.; Golderer, G.; Grobner, P.; Werner-Felmayer, G.; Werner, E.R.
Physarum polycephalum expresses a dihydropteridine reductase with selectivity for pterin substrates with a 6-(1', 2'-dihydroxypropyl) substitution
Biol. Chem.
384
1057-1062
2003
Physarum polycephalum (Q8WTJ2), Physarum polycephalum
brenda
Wilquet, V.; Van de Casteele, M.; Gigot, D.; Legrain, C.; Glansdorff, N.
Dihydropteridine reductase as an alternative to dihydrofolate reductase for synthesis of tetrahydrofolate in Thermus thermophilus
J. Bacteriol.
186
351-355
2004
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
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 (P09417), Homo sapiens
brenda
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
brenda
Schormann, N.; Pal, B.; Senkovich, O.; Carson, M.; Howard, A.; Smith, C.; Delucas, L.; Chattopadhyay, D.
Crystal structure of Trypanosoma cruzi pteridine reductase 2 in complex with a substrate and an inhibitor
J. Struct. Biol.
152
64-75
2005
Trypanosoma cruzi
brenda
Perez-Reinado, E.; Roldan, M.D.; Castillo, F.; Moreno-Vivian, C.
The NprA nitroreductase required for 2,4-dinitrophenol reduction in Rhodobacter capsulatus is a dihydropteridine reductase
Environ. Microbiol.
10
3174-3183
2008
Rhodobacter capsulatus
brenda
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
brenda
Chen, C.; Seo, K.H.; Kim, H.L.; Zhuang, N.; Park, Y.S.; Lee, K.H.
Crystallization and preliminary characterization of dihydropteridine reductase from Dictyostelium discoideum
Acta Crystallogr. Sect. F
64
1013-1015
2008
Dictyostelium discoideum
brenda
Lee, C.K.; Han, J.S.; Won, K.J.; Jung, S.H.; Park, H.J.; Lee, H.M.; Kim, J.; Park, Y.S.; Kim, H.J.; Park, P.J.; Park, T.K.; Kim, B.
Diminished expression of dihydropteridine reductase is a potent biomarker for hypertensive vessels
Proteomics
9
4851-4858
2009
Rattus norvegicus
brenda
Manjarrez-Gutierrez, G.; Gonzalez-Ramirez, M.; Boyzo-Montes de Oca, A.; Hernandez-Rodriguez, J.
Dihydropteridine reductase activity in the brainstem of intrauterine growth-restricted rats
Int. J. Dev. Neurosci.
28
621-624
2010
Rattus norvegicus
brenda
Gu, Y.; Gong, Y.; Zhang, H.; Dong, X.; Zhao, T.; Burczynski, F.J.; Wang, G.; Sun, S.; Zhu, B.; Han, W.; Wang, H.; Li, P.
Regulation of transforming growth factor beta 1 gene expression by dihydropteridine reductase in kidney 293T cells
Biochem. Cell Biol.
91
187-193
2013
Rattus norvegicus
brenda
Chen, C.; Kim, H.L.; Zhuang, N.; Seo, K.H.; Park, K.H.; Han, C.D.; Park, Y.S.; Lee, K.H.
Structural insights into the dual substrate specificities of mammalian and Dictyostelium dihydropteridine reductases toward two stereoisomers of quinonoid dihydrobiopterin
FEBS Lett.
585
2640-2646
2011
Dictyostelium discoideum (Q86A17), Dictyostelium discoideum
brenda
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)
brenda
Li, W.; Gong, M.; Shu, R.; Li, X.; Gao, J.; Meng, Y.
Molecular and enzymatic characterization of two enzymes BmPCD and BmDHPR involving in the regeneration pathway of tetrahydrobiopterin from the silkworm Bombyx mori
Comp. Biochem. Physiol. B
186
20-27
2015
Bombyx mori
brenda
Xu, Y.; Li, Y.; Li, L.; Zhang, L.; Ding, Z.; Shi, G.
Reductase-catalyzed tetrahydrobiopterin regeneration alleviates the anti-competitive inhibition of tyrosine hydroxylation by 7,8-dihydrobiopterin
Catal. Sci. Technol.
11
3128-3140
2021
Escherichia coli (P38489)
-
brenda