School of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, United Kingdom.
Org Biomol Chem. 2011 Oct 21;9(20):6920-3. doi: 10.1039/c1ob06184d. Epub 2011 Aug 25.
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.
对罗伊氏乳杆菌(P. roqueforti)aristolochene 合酶突变体产生的产物进行分析,揭示了脂族残基亮氨酸 108 在维持法呢基二磷酸的生产构象以确保 C1-C10(σ键)环合以及因此(+)-aristolochene 产生方面所起的重要结构作用。