CYP505E3: A Novel Self-Sufficient ω-7 In-Chain Hydroxylase.
The self-sufficient cytochrome P450 monooxygenase CYP505E3 from Aspergillus terreus catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the ω-7 position. It is the first reported P450 to give regioselective in-chain ω-7 hydroxylation of C10-C16 n-alkanes, thereby enabling the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. It shows more than 70 % regioselectivity for the eighth carbon from one methyl terminus, and displays remarkably high activity towards decane (TTN≈8000) and dodecane (TTN≈2000). CYP505E3 can be used to synthesize the high-value flavour compound δ-dodecalactone via two routes: 1) conversion of dodecanoic acid into 5-hydroxydodecanoic acid (24 % regioselectivity), which at low pH lactonises to δ-dodecalactone, and 2) conversion of 1-dodecanol into 1,5-dodecanediol (55 % regioselectivity), which can be converted into δ-dodecalactone by horse liver alcohol dehydrogenase.
['Maseme|Mpeyake Jacob|MJ|', 'Pennec|Alizé|A|', 'van Marwijk|Jacqueline|J|0000-0002-5350-4013', 'Opperman|Diederik Johannes|DJ|0000-0002-2737-8797', 'Smit|Martha Sophia|MS|0000-0002-1295-6507']
D000473:Alkanes D001230:Aspergillus D055162:Biocatalysis D003577:Cytochrome P-450 Enzyme System D005227:Fatty Acids D005233:Fatty Alcohols D006900:Hydroxylation D007783:Lactones D015394:Molecular Structure D011753:Pyrones D013379:Substrate Specificity
hydroxylation C−H activation biocatalysis cytochrome P450 enzymes lactones