Literature summary for 1.3.1.24 extracted from

Xu, Y.Q.; Ding, Z.K.
Biliverdin reductase from the liver of Atlantic salmon (Salmo salar) (2003), Biochemistry, 68, 639-643.

Search for more literature for 1.3.1.24

Inhibitors

Inhibitors	Comment	Organism	Structure
biliverdin IXalpha	with cofactor NADPH, inhibitory above 0.004 mM, with cofactor NADH, inhibitory above 0.018 mM	Salmo salar

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0006	-	biliverdin IXalpha	pH 7.0, 37°C, cosubstrate NADPH	Salmo salar
0.0068	-	biliverdin IXalpha	pH 7.0, 37°C, cosubstrate NADH	Salmo salar

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
68000	-	x * 68000, SDS-PAGE	Salmo salar

Organism

Organism	UniProt	Comment	Textmining
Salmo salar	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Salmo salar

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Salmo salar	-

Storage Stability

Storage Stability	Organism
-20°C, 50 mM potassium phosphate, pH 7.0, stable for at least eight months	Salmo salar

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
biliverdin IXalpha + NAD(P)H	-	Salmo salar	bilirubin + NAD(P)+	-	?

Subunits

Subunits	Comment	Organism
?	x * 68000, SDS-PAGE	Salmo salar

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
35	-	-	Salmo salar

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	cosubstrate NADPH	Salmo salar
6	-	cosubstrate NADH	Salmo salar

Cofactor

Cofactor	Comment	Organism	Structure
NAD(P)H	-	Salmo salar

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Release 2023.1 (January 2023)