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Literature summary for 1.5.1.30 extracted from

  • Redzic, J.S.; Duff, M.R.; Blue, A.; Pitts, T.M.; Agarwal, P.; Eisenmesser, E.Z.
    Modulating enzyme function via dynamic allostery within biliverdin reductase B (2021), Front. Mol. Biosci., 8, 691208 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens P30043
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Synonyms

Synonyms Comment Organism
biliverdin reductase B
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Homo sapiens
BLVRB
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Homo sapiens

General Information

General Information Comment Organism
evolution a position 15 A away from the active site within human biliverdin reductase B (T164) is inherently dynamic and can be mutated to control global micro-millisecond motions and function. By comparing the inherent dynamics through nuclear magnetic resonance (NMR) relaxation approaches of evolutionarily distinct biliverdin reductase B homologues and by applying Relaxation And Single Site Multiple Mutations (RASSMM) approach that monitors both the functional and dynamic effects of multiple mutations to the single T164 site, it is discovered that the most dramatic mutagenic effects coincide with evolutionary changes and these modulate coenzyme binding Homo sapiens
physiological function the enzyme is a critical players in cellular redox regulation Homo sapiens