title: Adenylate-forming enzymes.
abstract: Thioesters, amides, and esters are common chemical building blocks in a wide array of natural products. The formation of these bonds can be catalyzed in a variety of ways. For chemists, the use of an activating group is a common strategy and adenylate enzymes are exemplars of this approach. Adenylating enzymes activate the otherwise unreactive carboxylic acid by transforming the normal hydroxyl leaving group into adenosine monophosphate. Recently there have been a number of studies of such enzymes and in this review we suggest a new classification scheme. The review highlights the diversity in enzyme fold, active site architecture, and metal coordination that has evolved to catalyze this particular reaction.
authors.affiliation: Scottish Structural Proteomics Facility and Biomedical Science Research Complex, The University of St Andrews, Scotland KY16 9ST, UK.
authors.forename: Stefan
authors.initials: S
authors.lastname: Schmelz
authors.forename: James H
authors.initials: JH
authors.lastname: Naismith
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008670:Metals / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D004798:Enzymes; D008670:Metals; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate