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Literature summary extracted from

  • Firgaira, F.A.; Cotton, G.H.; Danks, D.M.
    Isolation and characterization of dihydropteridine reductase from human liver (1981), Biochem. J., 197, 31-43.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.34 5,5'-dithiobis(2-nitrobenzoate) 0.1 mM, 60% inhibition Homo sapiens
1.5.1.34 CoCl2 0.01 mM, 30% inhibition Homo sapiens
1.5.1.34 HgCl2 0.0001 mM, 60% inhibition Homo sapiens
1.5.1.34 iodoacetamide
-
 Homo sapiens
1.5.1.34 additional information not inhibited by EDTA, o-phenanthroline, and 2,2'-bipyridyl Homo sapiens
1.5.1.34 N-ethylmaleimide 1 mM, 76% inhibition Homo sapiens
1.5.1.34 p-chloromercuribenzoate 0.01 mM, 70% inhibition Homo sapiens
1.5.1.34 tetrahydrobiopterin above 0.05 mM, substrate inhibition Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.34 0.017
-
 tetrahydrobiopterin
-
 Homo sapiens
1.5.1.34 0.029
-
 NADH
-
 Homo sapiens
1.5.1.34 0.036
-
 2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
-
 Homo sapiens
1.5.1.34 0.77
-
 NADPH
-
 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.34 26000
-
 2 * 26000, SDS-PAGE Homo sapiens
1.5.1.34 47500
-
-
 Homo sapiens
1.5.1.34 50000
-
-
 Homo sapiens
1.5.1.34 54000
-
 gradient PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.34 quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H Homo sapiens essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan 5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.34 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.34
-
 Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.34 liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.34 422
-
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.34 2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H NADH is 20fold more effective than NADPH Homo sapiens 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
-
 ?
1.5.1.34 6,7-dihydropteridine + NADH
-
 Homo sapiens (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
-
 ?
1.5.1.34 quinoid dihydrobiopterin + NAD(P)H NADH is 2.5fold more effective than NADPH Homo sapiens tetrahydrobiopterin + NAD(P)+
-
 ?
1.5.1.34 quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan Homo sapiens 5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.34 dimer 2 * 26000, SDS-PAGE Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.34 37
-
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.34 200
-
 tetrahydrobiopterin
-
 Homo sapiens
1.5.1.34 510
-
 2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.34 7.2
-
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.34 NADH utilizes both NADH and NADPH Homo sapiens
1.5.1.34 NADH enzyme prefers NADH Homo sapiens
1.5.1.34 NADPH utilizes both NADH and NADPH Homo sapiens
1.5.1.34 NADPH NADH is preferred Homo sapiens