Cloned (Comment) | Organism |
---|---|
gene bluB, genotyping | Sinorhizobium meliloti |
Protein Variants | Comment | Organism |
---|---|---|
A156V | site-directed mutagenesis, inactive mutant | Sinorhizobium meliloti |
D32N | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Sinorhizobium meliloti |
D32N/S167G | site-directed mutagenesis, the mutant shows no activity | Sinorhizobium meliloti |
E78K | site-directed mutagenesis, the mutant is not soluble | Sinorhizobium meliloti |
G110S | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
G133S | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
G193D | site-directed mutagenesis, inactive mutant | Sinorhizobium meliloti |
G61D | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
M140I | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Sinorhizobium meliloti |
M94I | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Sinorhizobium meliloti |
P202L | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
P65L | site-directed mutagenesis, inactive mutant | Sinorhizobium meliloti |
R30C | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
R30H | site-directed mutagenesis, the mutant shows no 5,6-dimethylbenzimidazole forming activity | Sinorhizobium meliloti |
S167G | site-directed mutagenesis, the mutant shows higly reduced activity compared to the wild-type enzyme | Sinorhizobium meliloti |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | FMN/FMNH2 dissociation constants and free energy of binding of wild-type and mutant enzymes, overview | Sinorhizobium meliloti |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NADH + H+ + O2 | Sinorhizobium meliloti | - |
5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ? | 5,6-dimethylbenzimidazole is the lower axial ligand of vitamin B12, i.e. cobalamin | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sinorhizobium meliloti | Q92PC8 | gene bluB | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NADH + H+ + O2 | - |
Sinorhizobium meliloti | 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ? | 5,6-dimethylbenzimidazole is the lower axial ligand of vitamin B12, i.e. cobalamin | ? | |
FMNH2 + NADH + H+ + O2 | BluB fragments a flavin isoalloxazine ring | Sinorhizobium meliloti | 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BluB | - |
Sinorhizobium meliloti |
flavin destructase | - |
Sinorhizobium meliloti |
flavin destructase enzyme | - |
Sinorhizobium meliloti |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Sinorhizobium meliloti |
General Information | Comment | Organism |
---|---|---|
additional information | identification of catalytic residues involved in the reaction, mutational analysis, overview. The enzyme shows interactions with the phosphate group and ribityl tail of FMN | Sinorhizobium meliloti |