title: On the origin of enzymatic species.
abstract: The diversity of enzyme catalytic function is remarkable, particularly when one considers that ancestral life forms must have started with a much smaller ensemble of proteins. In this article, we discuss the evolution of the mandelate pathway in pseudomonads as an example of how catalytic diversity may have evolved. We suggest that existing enzymes that catalyse the chemistry needed to accomplish a transformation were recruited, followed by the evolution of specific binding.
authors.affiliation: Rosensteil Center, Brandeis University, Waltham, MA 02254.
authors.forename: G A
authors.initials: GA
authors.lastname: Petsko
authors.forename: G L
authors.initials: GL
authors.lastname: Kenyon
authors.forename: J A
authors.initials: JA
authors.lastname: Gerlt
authors.forename: D
authors.initials: D
authors.lastname: Ringe
authors.forename: J W
authors.initials: JW
authors.lastname: Kozarich
mesh_terms: D001665:Binding Sites; D005075:Biological Evolution; D008333:Mandelic Acids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000201:enzymology; D019998:Racemases and Epimerases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
chemical_list: D008333:Mandelic Acids; D019998:Racemases and Epimerases; C021540:mandelate racemase