BluB cannibalizes flavin to form the lower ligand of vitamin B12

Michiko E. Taga, Nicholas A. Larsen, Annaleise R. Howard-Jones, Christopher T. Walsh () and Graham C. Walker ()
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Michiko E. Taga: Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
Nicholas A. Larsen: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Annaleise R. Howard-Jones: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Christopher T. Walsh: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Graham C. Walker: Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA

Nature, 2007, vol. 446, issue 7134, 449-453

Abstract: The long road to vitamin B12 Vitamin B12 (cobalamin) is one of the largest known non-polymeric natural products, and it is the only vitamin that is synthesized exclusively by microorganisms. Despite years of study, the biosynthesis of one part of the vitamin is poorly understood. Now the last unknown step in its biosynthesis is revealed. The X-ray crystal structure of BluB, an enzyme that uses molecular oxygen to cleave a flavin mononucleotide cofactor to form the lower ligand of vitamin B12, has been determined. This reaction is an example of an unusual process, the enzymatic destruction of one cofactor to synthesize another.

Date: 2007
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DOI: 10.1038/nature05611

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