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Information on EC 1.13.11.79 - aerobic 5,6-dimethylbenzimidazole synthase and Organism(s) Propionibacterium freudenreichii and UniProt Accession D7GJ95

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IUBMB Comments
The enzyme catalyses a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12. This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor . The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. While D-erythrose 4-phosphate has been shown to be one of the byproducts, the nature of the other product(s) has not been verified yet.
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Propionibacterium freudenreichii
UNIPROT: D7GJ95
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
blub/cobt2, dmb-synthase, flavin destructase, more
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
FMNH2 oxidoreductase (5,6-dimethylbenzimidazole forming)
The enzyme catalyses a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12. This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor [4]. The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. While D-erythrose 4-phosphate has been shown to be one of the byproducts, the nature of the other product(s) has not been verified yet.