Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from actinomycetes.
The hydroxylation of alpha-ionone 1 and beta-ionone 2 to their corresponding mono-hydroxylated derivatives has been examined using a recombinant E. coli whole cell system, in which cytochromes P450 SU1 and SU2, and P450 SOY were over-expressed with their cognate ferrodoxins. Both substrates are hydroxylated with a high degree of regioselectivity and for alpha-ionone 1 the reaction is highly diastereoselective yielding the anti-isomer.
Celik
Ayhan
A
School of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK.
Flitsch
Sabine L
SL
Turner
Nicholas J
NJ
D039903:Actinobacteria / Q000201:enzymology*; D001711:Biotransformation; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000502:physiology*; D006900:Hydroxylation; D045792:Norisoprenoids / Q000378:metabolism*; D013237:Stereoisomerism
D045792:Norisoprenoids; D003577:Cytochrome P-450 Enzyme System; C008157:beta-ionone; C011879:alpha-ionone