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Crystal structure of an enzyme from Penicillium herquei in condition2Crystal structure of an enzyme from Penicillium herquei in condition2
Structural highlights
Publication Abstract from PubMedHydroalkoxylation 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. Crystal structure and proposed mechanism of an enantioselective hydroalkoxylation enzyme from Penicillium herquei.,Feng Y, Yu X, Huang JW, Liu W, Li Q, Hu Y, Yang Y, Chen Y, Jin J, Li H, Chen CC, Guo RT Biochem Biophys Res Commun. 2019 Aug 27;516(3):801-805. doi:, 10.1016/j.bbrc.2019.06.100. Epub 2019 Jun 27. PMID:31256936[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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