期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 9, 期 20, 页码 6920-6923出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1ob06184d
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资金
- United Kingdom's Biotechnology and Biological Sciences Research Council [BB/G003572/1, BB/H01683X/1]
- Engineering and Physical Sciences Research Council [EP/D06958/1]
- BBSRC [BB/G003572/1, BB/H01683X/1] Funding Source: UKRI
- EPSRC [EP/D069580/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G003572/1, BB/H01683X/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/D069580/1] Funding Source: researchfish
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 (sigma-bond) ring-closure and hence (+)-aristolochene production.
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