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Literature summary for 1.5.1.34 extracted from

  • Webber, S.; Hural, J.A.; Whiteley, J.M.
    Multiple forms of rat-liver dihydropteridine reductase identified by their differing isoelectric points (1986), Arch. Biochem. Biophys., 248, 358-367.
    View publication on PubMed

General Stability

General Stability Organism
stable to freezing at -70°C and thawing Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0025
-
quinonoid dihydrobiopterin enzyme form III Rattus norvegicus
0.0028
-
quinonoid dihydrobiopterin enzyme form I Rattus norvegicus
0.00285
-
quinonoid dihydrobiopterin enzyme form II Rattus norvegicus
0.0037
-
NADH enzyme form III Rattus norvegicus
0.00441
-
NADH enzyme form II Rattus norvegicus
0.0055
-
NADH enzyme form I Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25500
-
2 * 25500, SDS-PAGE Rattus norvegicus
25500
-
alpha,alpha, 2 * 25500, alpha,beta, 2 * 25500, beta,beta, 2 * 25500, 2 distinct subunits alpha and beta identified, the forms I, II and III represent three different dimeric combinations, SDS-PAGE Rattus norvegicus
51000
-
gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
multiple forms: I, II, II
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Storage Stability

Storage Stability Organism
4°C, stable for up to 2 weeks Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
quinonoid dihydrobiopterin + NADH + H+
-
Rattus norvegicus 6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 25500, SDS-PAGE Rattus norvegicus
dimer alpha,alpha, 2 * 25500, alpha,beta, 2 * 25500, beta,beta, 2 * 25500, 2 distinct subunits alpha and beta identified, the forms I, II and III represent three different dimeric combinations, SDS-PAGE Rattus norvegicus