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Literature summary extracted from

  • Rosenbaum, K.; Schaffrath, B.; Hagen, W.R.; Jahnke, K.; Gonzalez, F.J.; Cook, P.F.; Schnackerz, K.D.
    Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase (1997), Protein Expr. Purif., 10, 185-191.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.1.2 Sulfide 8.0 mol acid-labile sulfide per mol of subunit Sus scrofa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.2 expression in Escherichia coli Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.2 5,6-dihydrouracil
-
Sus scrofa
1.3.1.2 ATP-ribose dead-end inhibition Sus scrofa
1.3.1.2 NADP+ competitive versus NADPH Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.2 0.001
-
Uracil
-
Sus scrofa
1.3.1.2 0.006
-
NADPH
-
Sus scrofa
1.3.1.2 0.0066
-
NADPH in presence of 2,6-dihydrouracil Sus scrofa
1.3.1.2 0.023
-
Uracil in presence of 2,6-dihydrouracil Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.1.2 Iron 2 [4Fe-4S] clusters per subunit with 9.0 mol iron per mol of subunit Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.2 107000
-
2 * 107000, SDS-PAGE Sus scrofa
1.3.1.2 214000
-
recombinant from E. coli, native PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.2 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.2 recombinant protein Sus scrofa

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.2 14
-
recombinant from Escherichia coli Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.2 uracil + NADPH
-
Sus scrofa 5,6-dihydrouracil + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.3.1.2 dimer 2 * 107000, SDS-PAGE Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.2 flavin contains 2 mol FMN and 2 mol FAD per mol of enzyme, tightly associated Sus scrofa
1.3.1.2 NADPH strictly dependent on Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.1.2 additional information
-
additional information inhibitory reactions between uracil, NADP+ and dihydrouracil Sus scrofa