title: New insight into the catalytic mechanism of chorismate mutases from structural studies.
abstract: Chorismate mutase catalyzes the rearrangement of chorismic acid to prephenic acid, which is the first committed step in the biosynthesis of aromatic amino acids. Its catalytic mechanism has been much studied, but is poorly understood. Recent structural information on enzymes from two species, and on an antibody that catalyzes the same reaction, has shed new light on this topic.
authors.affiliation: Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.
authors.forename: A Y
authors.initials: AY
authors.lastname: Lee
authors.forename: J D
authors.initials: JD
authors.lastname: Stewart
authors.forename: J
authors.initials: J
authors.lastname: Clardy
authors.forename: B
authors.initials: B
authors.lastname: Ganem
mesh_terms: D000818:Animals; D002384:Catalysis; D002826:Chorismate Mutase / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D002826:Chorismate Mutase