Biliverdin Reductase B (human, recombinant)

Biliverdin reductase B, also known as S-nitroso-CoA-assisted nitrosyltransferase (SCAN), is an NADPH-dependent reductase and S-nitroso-CoA-dependent nitrosyltransferase encoded by BLVRB in humans that has roles in heme metabolism and insulin signaling.^1,2 It is a monomeric enzyme composed of a dinucleotide-binding domain that binds both NADPH and a substrate.¹ It is expressed in the liver and in erythrocytes and localizes to the cytoplasm.^3,2 Biliverdin reductase B uses NADPH as an electron donor to reduce biliverdin-IXβ to bilirubin in the last step of heme degradation during fetal development.^1,4 It can also reduce biliverdin-IXγ and biliverdin-IXδ, but not biliverdin-IXα, which is the predominant isoform in adults, as well as flavins, such as flavin mononucleotide (FMN), and ferric iron. Using S-nitroso-CoA (SNO-CoA) as a cofactor, biliverdin reductase B transfers SNO to cysteine residues in target proteins, such as the insulin receptor (InsR) and insulin receptor substrate 1 (IRS-1), which reduces insulin signaling.² Human skeletal muscle, visceral adipose, and subcutaneous adipose levels of biliverdin reductase B are positively associated with increased SNO-InsRβ levels in these tissues and with body mass index (BMI). Intratumoral levels of biliverdin reductase B are increased in comparison with levels in non-cancerous tissue in patients with esophageal carcinoma, endometrial carcinoma, or pancreatic cancer, among other cancers.⁵ A serine-to-leucine substitution at residue 111 of biliverdin reductase B inhibits its activity for both biliverdins and flavins and is a risk factor for thrombocytosis in humans.⁶ Cayman’s Biliverdin Reductase B (human, recombinant) protein can be used for ELISA, enzyme activity assay, and Western blot applications.

WARNING This product is not for human or veterinary use.

1. Nesbitt, N.M., Zheng, X., Li, Z., et al. In silico and crystallographic studies identify key structural features of biliverdin IXβ reductase inhibitors having nanomolar potency. The Journal of Biological Chemisty 293(15), 5431-5446 (2018).

2. Zhou, H.-L., Grimmett, Z.W., Venetos, N.M., et al. An enzyme that selectively S-nitrosylates proteins to regulate insulin signaling. Cell 186, 5812-5825 (2023).

3. Chikuba, K., Yubisui, T., Shirabe, K., et al. Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase. Biochem. Biophys. Res. Commun. 198(3), 1170-1176 (1994).

4. Pereira, P.J., Macedo-Ribeiro, S., Párraga, A., et al. Structure of human biliverdin IXβ reductase, an early fetal bilirubin IXβ producing enzyme. Nat. Struct. Biol. 8(3), 215-220 (2001).

5. Bahou, W.F., Marchenko, N., and Nesbitt, N.M. Metabolic functions of biliverdin IXβ reductase in redox-regulated hematopoietic cell fate. Antioxidants (Basel) 12(5), 1058 (20223).

6. Wu, S., Li, Z., Gnatenko, D.V., et al. BLVRB redox mutation defines heme degradation in a metabolic pathway of enhanced thrombopoiesis in humans. Blood 128(5), 699-709 (2016).