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Results 1 - 4 of 4
EC Number
General Information
BluB/CobT2 is the crucial enzyme in the B12 biosynthetic pathway of Propionibacterium freudenreichii
physiological function
a Tn5 insertion mutant is unable to grow in minimal media and fails to establish a symbiosis with alfalfa. Effect can be rescued by addition of vitamin B12 or of 5,6-dimethylbenzimidazole. Mutant does not produce cobalamin unless 5,6-dimethylbenzimidazole is supplied
physiological function
enzyme deletion mutant is unable to convert Mg-protoporphyrin IX monomethyl ester into protochlorophyllide, mutant starin grows poorly under anoxic photoheterotrophic conditions
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
Results 1 - 4 of 4