title: Modular evolution of the purine biosynthetic pathway.
abstract: Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in channeling of chemically unstable intermediates have all been examined in the past few years.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue 18-409, Cambridge, MA 02139, USA. kappock@wuchem.wustl.edu
authors.forename: T J
authors.initials: TJ
authors.lastname: Kappock
authors.forename: S E
authors.initials: SE
authors.lastname: Ealick
authors.forename: J
authors.initials: J
authors.lastname: Stubbe
mesh_terms: D019143:Evolution, Molecular; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry; D011687:Purines / Q000096:biosynthesis* / Q000737:chemistry
chemical_list: D011506:Proteins; D011687:Purines