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The final step in heme metabolism in mammals is catalyzed by the cytosolic biliverdin reductase enzymes A and B (EC 18.104.22.168).. Additionally we are shipping Flavin Reductase Antibodies (100) and Flavin Reductase Proteins (13) and many more products for this protein.
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Early stages of lineage fate potential require glutamine anaplerotic functions and an intact Pentose phosphate pathway, which are, in part, regulated by BLVRB activity. In principle, BLVRB inhibition represents an alternative strategy for modulating cellular glutamine utilization with consequences for cancer and hematopoietic metabolism.
These results provide promising chemical scaffolds for the development of enhanced BLVRB inhibitors and identify chemical probes to better dissect the role of biliverdins, alternative substrates, and BLVRB function in physiologically relevant cellular contexts.
These data define the first physiologically relevant function of BLVRB and implicate its activity and/or heme-regulated BV tetrapyrrole(s) in a unique redox-regulated bioenergetic pathway.
miR-127-5p suppressed NF-kappaB activity by directly targeting BLVRB in hepatocellular carcinoma cells.
Data suggest that isoenzymes BVRA and BVRB play different roles in energy metabolism and in pathogenesis of abdominal obesity and hypertriglyceridemia. [REVIEW]
quantum mechanics/molecular mechanics potential energy surfaces show that the lowest energy pathway proceeds with a positively charged pyrrole intermediate via two transition states
The final step in heme metabolism in mammals is catalyzed by the cytosolic biliverdin reductase enzymes A and B (EC 22.214.171.124).
, NADPH-dependent diaphorase
, NADPH-flavin reductase
, biliverdin-IX beta-reductase
, flavin reductase (NADPH)
, green heme-binding protein
, short chain dehydrogenase/reductase family 43U, member 1