Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P30043 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
biliverdin reductase B | - |
Homo sapiens |
BLVRB | - |
Homo sapiens |
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 |