EC Number   |
General Information |
Reference |
|---|
    1.5.1.30 | 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 |
764765 |
| 1.5.1.30 | evolution |
analysis of evolutionary or molecular mechanism of divergence of the nitroreductase/flavin reductase family, overview. The enzyme is similar to NfsA from Escherichia coli, overview |
-, 742109 |
| 1.5.1.30 | evolution |
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning |
765735 |
| 1.5.1.30 | evolution |
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning |
765735 |
| 1.5.1.30 | evolution |
most BLVRB enzymes have an arginine at either residue 14 or residue 78 (human numbering), although a subset maintain an arginine at both sites. In primates, the two substitutions are made on the same branch separating the common ancestor of the Simiiformes (apes, new and old-world monkeys) with the common ancestor of the Haplorhini (i.e., after the split from the common ancestor with the tarsier). This suggests possible adaptive coevolution at these two sites and adjusting the location of this arginine may serve to fine-tune coenzyme binding in BLVRB enzymes |
765238 |
| 1.5.1.30 | evolution |
the flavin reductase DNA sequence of the TIGR4 strain is compared to 29 completely sequenced genomes of Streptococcus pneumoniae. All 29 genomes contain a highly similar locus to SP_RS 02775 |
765814 |
| 1.5.1.30 | evolution |
the study elucidates the role of the evolutionarily changing biliverdin reductase (BBLVRB) active site that serves to modulate coenzyme release and shows that coenzyme release is coupled to substrate turnover |
765021 |
| 1.5.1.30 | malfunction |
a flaR mutant is highly susceptible to H2O2 compared to its wild-type and complemented strains, suggesting a role for FlaR in pneumococcal oxidative stress resistance. The flaR mutant demonstrates significantly decreased mice mortality following intraperitoneal infection. A lack of FlaR does not affect the extent of phagocytosis by primary mouse peritoneal macrophages but reduces adhesion to A549 cells compared to wild-type and complemented strains |
765814 |
| 1.5.1.30 | metabolism |
CysJ functions as a specific partner of the YcbX molybdoenzyme and provides the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter |
725248 |
| 1.5.1.30 | metabolism |
heme degradation enzyme biliverdin IXbeta reductase is required for stem cell glutamine metabolism |
764101 |
