title: Enzymes required for the biosynthesis of N-formylated sugars.
abstract: The N-formyltransferases, also known as transformylases, play key roles in de novo purine biosynthesis where they catalyze the transfer of formyl groups to primary amine acceptors. These enzymes require N10-formyltetrahydrofolate for activity. Due to their biological importance they have been extensively investigated for many years, and they are still serving as targets for antifolate drug design. Most of our understanding of the N-formyltransferases has been derived from these previous studies. It is now becoming increasingly apparent, however, that N-formylation also occurs on some amino sugars found on the O-antigens of pathogenic bacteria. This review focuses on recent developments in the biochemical and structural characterization of the sugar N-formyltransferases.
authors.affiliation: Department of Biochemistry, University of Wisconsin, Madison, WI 53706, United States. Electronic address: hazel_holden@biochem.wisc.edu.
authors.forename: Hazel M
authors.initials: HM
authors.lastname: Holden
authors.affiliation: Department of Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
authors.forename: James B
authors.initials: JB
authors.lastname: Thoden
authors.affiliation: Human Health Therapeutics, National Research Council Canada, Ottawa, Ontario K1A OR6, Canada.
authors.forename: Michel
authors.initials: M
authors.lastname: Gilbert
mesh_terms: D001419:Bacteria / Q000201:enzymology; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000096:biosynthesis*; D006801:Humans; D019877:Hydroxymethyl and Formyl Transferases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002241:Carbohydrates; D019877:Hydroxymethyl and Formyl Transferases