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Literature summary for 1.5.1.34 extracted from

  • Hirayama, K.; Nakanisi, N.; Sueoka, T.; Katoh, S.; Yamada, S.
    Dihydropteridine reductase and tetrahydropterin in Crithidia fasciculata cells (1980), Biochim. Biophys. Acta, 612, 337-343.
    View publication on PubMed
Search for more literature for 1.5.1.34

General Stability

General Stability Organism
not stable during gel filtration Crithidia fasciculata
unstable to (NH4)2SO4 precipitation Crithidia fasciculata

Inhibitors

Inhibitors Comment Organism Structure
aminopterin 1 mM, 50% inhibition Crithidia fasciculata
methopterin 1 mM, 10% inhibition Crithidia fasciculata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0028
-
 NADH
-
 Crithidia fasciculata
0.0088
-
 NADPH
-
 Crithidia fasciculata

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 gel filtration Crithidia fasciculata

Organism

Organism UniProt Comment Textmining
Crithidia fasciculata
-
-
-

Storage Stability

Storage Stability Organism
-80°C, 40 mM potassium phosphate buffer, pH 6.8, stable for at least a week Crithidia fasciculata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H more specific for NADH, 50% activity with NADPH, no activity with biopterin and 7,8-dihydrobiopterin Crithidia fasciculata 5,6,7,8-tetrahydrobiopterin + NAD(P)+
-
 ?
quinonoid dihydrobiopterin + NADH + H+
-
 Crithidia fasciculata 5,6,7,8-tetrahydrobiopterin + NAD+
-
 r

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5 8 unstable below and above Crithidia fasciculata

Cofactor

Cofactor Comment Organism Structure
NADH utilizes both NADH and NADPH Crithidia fasciculata
NADH enzyme prefers NADH Crithidia fasciculata
NADPH utilizes both NADH and NADPH Crithidia fasciculata
NADPH NADH is preferred Crithidia fasciculata