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Literature summary extracted from

  • Ding, Z.; Xu, Y.
    Purification and properties of cow splenic biliverdin reductase (1994), Prep. Biochem., 24, 193-201.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.24 Biliverdin
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.24 0.0004
-
 biliverdin IXalpha cosubstrate NADPH Bos taurus
1.3.1.24 0.0015
-
 biliverdin IXalpha cosubstrate NADH Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.24 34000
-
-
 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.24 Bos taurus
-
 cow
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.24
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.24 spleen
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.24 biliverdin + NAD(P)H specific for biliverdin and IXalpha faster than the biliverdin isomers IXbeta, IXr or IXdelta Bos taurus bilirubin + NAD(P)+
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.24 6.8
-
 biliverdin + NADPH Bos taurus
1.3.1.24 7
-
 biliverdin + NADH Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.24 NADH time-course of the NADH-dependent reaction displayes no sigmoidal curve Bos taurus
1.3.1.24 NADPH time-course of the NADPH-dependent reaction displayes a sigmoidal curve Bos taurus