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Significance Terpene synthases catalyze complex, chain length-specific, electrophilic cyclization reactions that constitute the first committed step in the biosynthesis of structurally diverse terpenoids. (4S )-limonene synthase [(4S )-LS] has emerged as a model enzyme for enhancing our comprehension of the reaction cycle of monoterpene (C10 ) synthases. While the stereochemistry of the cyclization of geranyl diphosphate to (−)-(4S )-limonene has been the subject of several mechanistic studies, the structural basis for the stabilization of carbocation intermediates and the termination of the reaction sequence have remained enigmatic. We present extensive experimental evidence that the aromatic amino acids W324 and H579 play critical roles in the stabilization of intermediate carbocations. A possible function of these residues as the terminal catalytic base is also discussed.

Functional analysis of (4 S )-limonene synthase mutants reveals determinants of catalytic outcome in a model monoterpene synthase