Templating effects in aristolochene synthase catalysis: elimination versus cyclisation

Analysis of the products generated by mutants of aristolochene synthase from P. roqueforti (PR-AS) revealed the prominent structural role played by the aliphatic residue Leu 108 in maintaining the productive conformation of farnesyl diphosphate to ensure C1–C10 (σ-bond) ring-closure and hence (+)-aristolochene production