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Literature summary extracted from
- Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis (1997), J. Biol. Chem., 272, 13562-13569.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.24 | expressed in Escherichia coli | Synechocystis sp. |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.24 | 0.0013 | - |
Biliverdin | enzyme has a 6-histidine-tagged amino-terminal fusion | Synechocystis sp. |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.24 | Synechocystis sp. | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.24 | biliverdin + NAD(P)H | - |
Synechocystis sp. | bilirubin + NAD(P)+ | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.24 | 5.8 | - |
biliverdin + NADPH | Synechocystis sp. |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.24 | NADH | - |
Synechocystis sp. | |
| 1.3.1.24 | NADPH | - |
Synechocystis sp. | |
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Release 2023.1 (January 2023)
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