title: Adenosyltransferase tailors and delivers coenzyme B12.
abstract: 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.
authors.affiliation: Biological Chemistry Department, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0606, USA.
authors.forename: Dominique
authors.initials: D
authors.lastname: Padovani
authors.forename: Tetyana
authors.initials: T
authors.lastname: Labunska
authors.forename: Bruce A
authors.initials: BA
authors.lastname: Palfey
authors.forename: David P
authors.initials: DP
authors.lastname: Ballou
authors.forename: Ruma
authors.initials: R
authors.lastname: Banerjee
mesh_terms: D000818:Animals; D001665:Binding Sites; D001692:Biological Transport; D002384:Catalysis; D003038:Cobamides / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008716:Methionine Adenosyltransferase / Q000737:chemistry / Q000378:metabolism*; D008765:Methylmalonyl-CoA Mutase / Q000737:chemistry / Q000378:metabolism*; D020601:Methylobacterium extorquens / Q000201:enzymology; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism
chemical_list: D003038:Cobamides; D018832:Molecular Chaperones; D008716:Methionine Adenosyltransferase; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide