title: Mechanistically diverse enzyme superfamilies: the importance of chemistry in the evolution of catalysis.
abstract: The strategy that nature has used to evolve new catalytic activities from pre-existing enzymes (i.e. retention of substrate binding or of catalytic mechanism) has been controversial. Recent work supports a strategy in which a partial reaction, catalyzed by a progenitor, is retained, and the active-site architecture is modified to allow the intermediate generated to be directed to different products.
authors.affiliation: Department of Biochemistry, University of Illinois at Urbana-Champaign 61801, USA. j-gerlt@uiuc.edu
authors.forename: J A
authors.initials: JA
authors.lastname: Gerlt
authors.forename: P C
authors.initials: PC
authors.lastname: Babbitt
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D001426:Bacterial Proteins; D005075:Biological Evolution; D002384:Catalysis; D004746:Enoyl-CoA Hydratase / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D005982:Glutathione Transferase / Q000737:chemistry / Q000145:classification / Q000235:genetics; D007791:Lactoylglutathione Lyase / Q000737:chemistry / Q000145:classification / Q000235:genetics; D008667:Metalloproteins / Q000737:chemistry / Q000145:classification / Q000235:genetics; D010105:Oxygenases / Q000737:chemistry / Q000145:classification / Q000235:genetics; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000145:classification / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D008667:Metalloproteins; D010105:Oxygenases; D005982:Glutathione Transferase; D000581:Amidohydrolases; D010751:Phosphopyruvate Hydratase; D004746:Enoyl-CoA Hydratase; D007791:Lactoylglutathione Lyase