Abstract
Two enzymes-mandelate racemase (MR) and muconate lactonizing enzyme (MLE)-that catalyze mechanistically distinct reactions have been shown to be structurally homologous, and thus very likely evolutionary related [ Nature , 347, 692 (1990)]. This is the first clear example of two enzymes that appear to have evolved from a common ancestor's catalyzing different chemical reactions, according to the chemists who carried out the research. MR and MLE are both part of a biochemical pathway that allows Pseudomonas putida to metabolize aromatic carboxylic acids. MR catalyzes the interconversion of two enantiomers. MLE catalyzes the cycloisomerization of cis,cis -muconic acid to muconolactone by syn addition to a double bond. The research was carried out by Gregory A. Petsko and David J. Neidhart of Massachusetts Institute of Technology, Cambridge; George L. Kenyon of the University of California, San Francisco; and John A. Gerlt of the University of Maryland, College Park. (Petsko has since moved to Brandeis Unive...
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