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Literature summary for 1.13.11.79 extracted from

  • Yu, T.Y.; Mok, K.C.; Kennedy, K.J.; Valton, J.; Anderson, K.S.; Walker, G.C.; Taga, M.E.
    Active site residues critical for flavin binding and 5,6-dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB (2012), Protein Sci., 21, 839-849.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene bluB, genotyping Sinorhizobium meliloti

Protein Variants

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q92PC8 gene bluB
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
BluB
-
Sinorhizobium meliloti
flavin destructase
-
Sinorhizobium meliloti
flavin destructase enzyme
-
Sinorhizobium meliloti

Cofactor

Cofactor Comment Organism Structure
NADH
-
Sinorhizobium meliloti

General Information

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