title: Novel product chemistry from mechanistic analysis of ent-copalyl diphosphate synthases from plant hormone biosynthesis.
abstract: An active-site water molecule coordinated by conserved histidine and asparagine residues seems to serve as the catalytic base in all ent-copalyl diphosphate synthases (CPSs). When these residues are substituted by alanine, the mutant CPSs produce stereochemically novel ent-8-hydroxy-CPP. Given the requisite presence of CPSs in all land plants for gibberellin phytohormone biosynthesis, such plasticity presumably underlies the observed extensive diversification of the resulting labdane-related diterpenoids.
authors.affiliation: Dept. Biochemistry, Biophysics & Molecular Biology, Iowa State University, Ames, IA 50011 (USA).
authors.forename: Kevin
authors.initials: K
authors.lastname: Potter
authors.forename: Jared
authors.initials: J
authors.lastname: Criswell
authors.forename: Jiachen
authors.initials: J
authors.lastname: Zi
authors.forename: Alisha
authors.initials: A
authors.lastname: Stubbs
authors.forename: Reuben J
authors.initials: RJ
authors.lastname: Peters
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000378:metabolism*; D001688:Biological Products / Q000737:chemistry; D008958:Models, Molecular; D010937:Plant Growth Regulators / Q000096:biosynthesis* / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D001688:Biological Products; D010937:Plant Growth Regulators; D010940:Plant Proteins; D019883:Alkyl and Aryl Transferases; C090963:ent-kaurene synthetase A
keywords: biosynthesis; cyclization; enzyme catalysis; natural products; reaction mechanism