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

BRENDA support

Literature summary extracted from

  • Porter, D.J.T.; Spector, T.
    Dihydropyrimidine dehydrogenase. Kinetic mechanism for reduction of uracil by NADPH (1993), J. Biol. Chem., 268, 19321-19327.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.2 5-Ethynyluracil suicide inactivator covalently modifying a cysteinyl residue Bos taurus
1.3.1.2 NADP+ competitive versus NADPH Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.2 0.00012
-
 NADPH
-
 Bos taurus
1.3.1.2 0.00012
-
 Uracil
-
 Bos taurus
1.3.1.2 0.0004
-
 NADP+ in presence of 5,6-dihydrouracil Bos taurus
1.3.1.2 0.0008
-
 Uracil cofactor NADPH Bos taurus
1.3.1.2 0.24
-
 5,6-dihydrouracil in presence of NADP+ Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.2 Bos taurus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.1.2 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+ random rapid-equilibrium mechanism Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.2 liver
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.2 5,6-dihydrouracil + NADP+
-
 Bos taurus uracil + NADPH
-
 r
1.3.1.2 thymine + NADPH
-
 Bos taurus dihydrothymine + NADP+
-
 r
1.3.1.2 uracil + NADPH
-
 Bos taurus 5,6-dihydrouracil + NADP+
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.2 0.4
-
 5,6-dihydrouracil
-
 Bos taurus
1.3.1.2 1.6
-
 Uracil
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.2 NADP+
-
 Bos taurus
1.3.1.2 NADPH
-
 Bos taurus