Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.34 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
Search for more literature for 1.5.1.34

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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)+
-
 ?
6,7-dihydropteridine + NADH
-
 Homo sapiens (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
-
 ?
quinoid dihydrobiopterin + NAD(P)H NADH is 2.5fold more effective than NADPH Homo sapiens tetrahydrobiopterin + NAD(P)+
-
 ?
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

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
 Homo sapiens

Cofactor

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