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

BRENDA support

Literature summary extracted from

  • Lovstad, R.A.
    A kinetic study on the phenothiazine dependent oxidation of NADH by bovine ceruloplasmin (2006), Biometals, 19, 1-5.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.16.3.1 chlorpromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
1.16.3.1 levopromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
1.16.3.1 promazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus
1.16.3.1 triflupromazine formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.3.1 0.14
-
 NADH pH 6.0, 30°C, presence of triflupromazine Bos taurus
1.16.3.1 0.21
-
 NADH pH 6.0, 30°C, presence of levomepromazine Bos taurus
1.16.3.1 0.22
-
 NADH pH 6.0, 30°C, presence of chlorpromazine Bos taurus
1.16.3.1 0.23
-
 NADH pH 6.0, 30°C, presence of promazine Bos taurus

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.3.1 NADH + O2
-
 Bos taurus NAD+ + H2O
-
 ?