Brief Communication abstract


Nature Chemical Biology 4, 194 - 196 (2008)
Published online: 10 February 2008 | doi:10.1038/nchembio.67

Adenosyltransferase tailors and delivers coenzyme B12

Dominique Padovani1,2, Tetyana Labunska2, Bruce A Palfey1, David P Ballou1 & Ruma Banerjee1,2

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The reactivity and relative rarity of most cofactors pose challenges for their delivery to target enzymes. Using kinetic analyses, we demonstrate that adenosyltransferase, which catalyzes the final step in the assimilation of coenzyme B12, directly transfers the cofactor to methylmalonyl coenzyme A mutase. The strategy of using the final enzyme in an assimilation pathway for tailoring a cofactor and delivering it to a dependent enzyme may be general for cofactor trafficking.

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  1. Biological Chemistry Department, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0606, USA.
  2. Redox Biology Center and Department of Biochemistry, University of Nebraska, 19th and Vine, Lincoln, Nebraska 68588-0664, USA.

Correspondence to: Ruma Banerjee1,2 e-mail: rbanerje@umich.edu



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