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Abstract | Cited by

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.

Graphical abstract: Templating effects in aristolochene synthase catalysis: elimination versus cyclisation

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