Atomic Structure of the Buried Catalytic Pocket of Escherichia coli Chorismate Mutase

摘要

The first committed step in the biosynthesis of the aromatic amino acids phenylalanine and tyrosine is the chorismate mutase-catalyzed conversion of chorismate (1) to prephenate (2). How the enzyme accelerates this pericyclic rearrangement by at least 10~6-fold is not well understood, and analysis has been complicated by the existence of many different chorismate mutases with low sequence identity and unknown structural similarity. Recently reported structures of the monofunctional chorismate mutase from Bacillus subtilis (BsCM), and the monofunctional allosteric chorismate mutase from yeast (Sac-charomyces cerevisiae, ScCM), presented important insights, but the extent of mechanistic and structural similarity among chorismate mutases remained unanswered.