Selective allylic hydroxylation of acyclic terpenoids by CYP154E1 from Thermobifida fusca YX.

ABSTRACT: Allylic alcohols are valuable precursors in the synthesis of pharmaceutical intermediates, agrochemicals and natural products. Regioselective oxidation of parental alkenes is a challenging task for chemical catalysts and requires several steps including protection and deprotection. Many cytochrome P450 enzymes are known to catalyse selective allylic hydroxylation under mild conditions. Here, we describe CYP154E1 from Thermobifida fusca YX that enables this type of oxidation. Several acyclic terpenoids were tested as possible substrates for CYP154E1, and the regio- and chemoselectivity of their oxidation was investigated. Using a previously established bioinformatics approach we identified position 286 in the active site of CYP154E1 which is putatively involved in substrate binding and ther

SUBMITTER: Bogazkaya AM 

PROVIDER: S-EPMC4077532 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature