Biotransformation of the sesquiterpene (+)-valencene by cytochrome P450cam and P450BM-3.

Journal article

The sesquiterpenoids are a large class of naturally occurring compounds with biological functions and desirable properties. Oxidation of the sesquiterpene (+)-valencene by wild type and mutants of P450cam from Pseudomonas putida, and of P450BM-3 from Bacillus megaterium, have been investigated as a potential route to (+)-nootkatone, a fine fragrance. Wild type P450cam did not oxidise (+)-valencene but the mutants showed activities up to 9.8 nmol (nmol P450)(-1) min(-1), with (+)-trans-nootkatol and (+)-nootkatone constituting >85% of the products. Wild type P450BM-3 and mutants had higher activities (up to 43 min(-1)) than P450cam but were much less selective. Of the many products, cis- and trans-(+)-nootkatol, (+)-nootkatone, cis-(+)-valencene-1,10-epoxide, trans-(+)-nootkaton-9-ol, and (+)-nootkatone-13S,14-epoxide were isolated from whole-cell reactions and characterised. The selectivity patterns suggest that (+)-valencene has one binding orientation in P450cam but multiple orientations in P450BM-3.

Authors: Sowden, R; Yasmin, S; Rees, N; Bell, S; Wong, L

• Publication status: Published
• Journal: Organic and biomolecular chemistry
• Volume: 3
• Issue: 1
• Pages: 57-64
• Publication date: 2005-01-01
• DOI: 10.1039/b413068e
• EISSN: 1477-0539
• ISSN: 1477-0520
• Language: English
• Keywords: Structure-Activity Relationship; Camphor 5-Monooxygenase; Oxidation-Reduction; Stereoisomerism; Models, Molecular; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Cytochrome P-450 Enzyme System; Bacillus megaterium; Biotransformation; Bacterial Proteins; Pseudomonas putida; Sesquiterpenes; Molecular Structure