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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
evolution
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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
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
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
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
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
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
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
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
evolution
XP_020138941.1
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
evolution
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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
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metabolism
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the flavin reductase couples with dibenzothiophene and dibenzothiophene sulfone monooxygenase in the thermophilic dibenzothiophene (DBT)-desulfurizing bacterium, the flavin reductase exhibits flavin reductase and nitroreductase activities
metabolism
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CysJ functions as a specific partner of the YcbX molybdoenzyme and provides the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter
metabolism
Trichomonas vaginalis has two different enzymatic pathways to remove intracellular oxygen, i.e. NADH oxidase, which is inhibited by metronidazole, and flavin reductase
metabolism
heme degradation enzyme biliverdin IXbeta reductase is required for stem cell glutamine metabolism
metabolism
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
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the flavin reductase couples with dibenzothiophene and dibenzothiophene sulfone monooxygenase in the thermophilic dibenzothiophene (DBT)-desulfurizing bacterium, the flavin reductase exhibits flavin reductase and nitroreductase activities
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metabolism
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Trichomonas vaginalis has two different enzymatic pathways to remove intracellular oxygen, i.e. NADH oxidase, which is inhibited by metronidazole, and flavin reductase
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physiological function
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provides reducing equivalents required to drive the luciferase genes in Escherichia coli but is not coupled to luciferase
physiological function
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CysJ is involved in 6-N-hydroxylaminopurine resistance
physiological function
regarding all flavin reductase enzymes in Trichomonas vaginalis, FR1 is responsible for the flavin reductase activity. Hydrogen peroxide is the main if not the single product of FR1. FR1 displays a 10 to 20fold higher affinity to FMN than enzymes FR5 and FR6. Also the affinity of FR1 to FAD is at least 10fold higher than observed with FR5 and FR6 but the Vmax is considerably lower (roughly 33% of the Vmax for FMN). In contrast, FR5 and FR6 display higher affinity for riboflavin than FR1, which is inhibited by riboflavin
physiological function
flavin reductase contributes to pneumococcal virulence by protecting from oxidative stress and mediating adhesion and elicits protection against pneumococcal challenge, role for FlaR in pneumococcal oxidative stress resistance. FlaR involvement in virulence i.e. adhesion to host cells, mechanism, overview
physiological function
the enzyme is a critical players in cellular redox regulation
physiological function
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regarding all flavin reductase enzymes in Trichomonas vaginalis, FR1 is responsible for the flavin reductase activity. Hydrogen peroxide is the main if not the single product of FR1. FR1 displays a 10 to 20fold higher affinity to FMN than enzymes FR5 and FR6. Also the affinity of FR1 to FAD is at least 10fold higher than observed with FR5 and FR6 but the Vmax is considerably lower (roughly 33% of the Vmax for FMN). In contrast, FR5 and FR6 display higher affinity for riboflavin than FR1, which is inhibited by riboflavin
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additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases