title: Templating effects in aristolochene synthase catalysis: elimination versus cyclisation.
abstract: 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.
authors.affiliation: School of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, United Kingdom.
authors.forename: Juan A
authors.initials: JA
authors.lastname: Faraldos
authors.forename: Verónica
authors.initials: V
authors.lastname: González
authors.forename: Michael
authors.initials: M
authors.lastname: Senske
authors.forename: Rudolf K
authors.initials: RK
authors.lastname: Allemann
mesh_terms: D055162:Biocatalysis; D020134:Catalytic Domain; D003500:Cyclization; D007535:Isomerases / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D010407:Penicillium / Q000201:enzymology* / Q000235:genetics; D012717:Sesquiterpenes / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D012717:Sesquiterpenes; C054277:aristolochene; D007535:Isomerases; C060050:aristolochene synthase