benzofurans and herquienone

Hydroalkoxylation is a useful and efficient reaction which generates C-O bond and produces cyclic ethers, the common structural elements of natural products. The dedicative enzyme which can catalyze enantioselective hydroalkoxylation named PhnH was recently identified in the herqueinone biosynthetic gene from Penicillium herquei. It catalyzes addition of a phenol to the terminal olefin on substrate to produce a dihydrobenzofuran. Here, the crystal structure of PhnH is reported and the putative substrate-binding pocket is illustrated. Through docking experiment, possible substrate-binding poses are displayed and the catalytic mechanism is therefore proposed. Our findings form the basis for further studies of enantioselective hydroalkoxylation enzymes.

Topics: Alcohols; Benzofurans; Binding Sites; Catalysis; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Ethers, Cyclic; Fungal Proteins; Gene Expression; Genetic Vectors; Molecular Docking Simulation; Penicillium; Phenalenes; Phenols; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Stereoisomerism; Substrate Specificity