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Literature summary for 1.3.1.24 extracted from

  • Fu, G.; Liu, H.; Doerksen, R.J.
    Molecular modeling to provide insight into the substrate binding and catalytic mechanism of human biliverdin-IXalpha reductase (2012), J. Phys. Chem. B, 116, 9580-9594.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+ induced fit docking is emplyed to study the substrate binding modes to hBVR-A of biliverdin-IXalpha and four analogues. Substrate binding modes are examined further by performing molecular dynamics (MD) simulations followed by molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) calculations. On the basis of our calculations, the energetically preferred pathway consists of an initial protonation of the pyrrolic nitrogen on the biliverdin substrate followed by hydride transfer to yield the reduction product Homo sapiens

Synonyms

Synonyms Comment Organism
hBVR-A
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Homo sapiens