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Literature summary for 1.13.11.79 extracted from

  • Deptula, P.; Kylli, P.; Chamlagain, B.; Holm, L.; Kostiainen, R.; Piironen, V.; Savijoki, K.; Varmanen, P.
    BluB/CobT2 fusion enzyme activity reveals mechanisms responsible for production of active form of vitamin B12 by Propionibacterium freudenreichii (2015), Microb. Cell Fact., 14, 186 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene bluB/cobT2, a natural fusion gene coding for a predicted phosphoribosyltransferase/nitroreductase, sequence comparisons, recombinant expression of HaloTag-tagged enzyme in Escherichia coli strain KRX Propionibacterium freudenreichii subsp. shermanii

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii D7GJ95
-
-
Propionibacterium freudenreichii subsp. shermanii DSM 4902 D7GJ95
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant HaloTag-tagged enzyme from Escherichia coli strain KRX Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMNH2 + O2
-
Propionibacterium freudenreichii subsp. shermanii 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
?
FMNH2 + O2
-
Propionibacterium freudenreichii subsp. shermanii DSM 4902 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
-
?

Synonyms

Synonyms Comment Organism
BluB
-
Propionibacterium freudenreichii subsp. shermanii
bluB/cobT2
-
Propionibacterium freudenreichii subsp. shermanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Propionibacterium freudenreichii subsp. shermanii

General Information

General Information Comment Organism
metabolism BluB/CobT2 is the crucial enzyme in the B12 biosynthetic pathway of Propionibacterium freudenreichii Propionibacterium freudenreichii subsp. shermanii
physiological function the enzyme is involved in production of vitamin B12, a prerequisite for attempts to naturally fortify foods with B12 by microbial fermentation. Active vitamin B12 is distinguished from the pseudovitamin by the presence of 5,6-dimethylbenzimidazole (DMBI) as the lower ligand. Fusion enzyme BluB/CobT2 is efficient in metabolite channeling, and the enzymes' inability to react with adenine, a lower ligand present in the pseudovitamin, reveals a mechanism favoring the production of the active form of the vitamin, requirement of oxygen for DMBI synthesis, since the organism does not synthesize cobalamin. BluB is responsible for the formation of DMBI from FMNH2 in the presence of oxygen, BluB/CobT2 activates DMBI into alpha-RP in the presence of NaMN Propionibacterium freudenreichii subsp. shermanii