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Literature summary extracted from

  • Frydman, R.B.; Tomaro, M.L.; Rosenfeld, J.; Awruch, J.; Sambrotta, L.; Valasinas, A.; Frydman, B.
    Biliverdin reductase: substrate specificity and kinetics (1987), Biochim. Biophys. Acta, 916, 500-511.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.24 0.023
-
 biliverdin IXalpha
-
 Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.24 54000
-
 liver (form 2), HPLC Rattus norvegicus
1.3.1.24 68000
-
 liver (form 3), HPLC 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 two and four propionates in the biliverdin structure give a biliverdin with substrate activity but biliverdins carrying methyl, ethyl and one propionate residue in their structure and biliverdins with one propionate and one acetate residue or with two acetate residues are no substrates 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