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

BRENDA support

Literature summary extracted from

  • Bell, J.E.; Maines, M.D.
    Kinetic properties and regulation of biliverdin reductase (1988), Arch. Biochem. Biophys., 263, 1-9.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.24 bilirubin product inhibition Rattus norvegicus
1.3.1.24 Iron-hematoporphyrin competitive, acts as biliverdin-bilirubin analog Rattus norvegicus
1.3.1.24 NAD+ product inhibition Rattus norvegicus
1.3.1.24 NADP+ product inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.24 0.0069
-
Biliverdin at pH 7 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.24 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.24 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.24 biliverdin + NAD(P)H
-
Rattus norvegicus bilirubin + NAD(P)+
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.24 NADH
-
Rattus norvegicus
1.3.1.24 NADPH
-
Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.1.24 0.0019
-
NAD+ at pH 7 Rattus norvegicus
1.3.1.24 0.0098
-
bilirubin at pH 7 Rattus norvegicus
1.3.1.24 0.0454 0.583 NADP+ at pH 8.7 Rattus norvegicus