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10.1021/acs.joc.5b01951

http://scihub22266oqcxt.onion/10.1021/acs.joc.5b01951
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C4806863!4806863!26495876
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suck abstract from ncbi

pmid26495876      J+Org+Chem 2015 ; 80 (23): 11672-85
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  • Natural Diels-Alderases: Elusive and Irresistable #MMPMID26495876
  • Klas K; Tsukamoto S; Sherman DH; Williams RM
  • J Org Chem 2015[Dec]; 80 (23): 11672-85 PMID26495876show ga
  • Eight examples of biosynthetic pathways wherein a natural enzyme has been identified and claimed to function as a catalyst for the [4+2] cycloaddition reaction, namely, Diels-Alderases, are briefly reviewed. These are discussed in the context of the mechanistic challenges associated with the technical difficulty of proving that the net formal [4+2] cycloaddition under study, indeed proceeds through a synchronous, mechanism and that the putative biosynthetic enzyme deploys the pericyclic transition state required for a Diels-Alder cycloaddition reaction.
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