[
    {
        "id": "authors:59g54-8es80",
        "collection": "authors",
        "collection_id": "59g54-8es80",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20160317-072334231",
        "type": "article",
        "title": "Asymmetric Enzymatic Synthesis of Allylic Amines: A Sigmatropic Rearrangement Strategy",
        "author": [
            {
                "family_name": "Prier",
                "given_name": "Christopher K.",
                "orcid": "0000-0003-0902-1636",
                "clpid": "Prier-Christopher-K"
            },
            {
                "family_name": "Hyster",
                "given_name": "Todd K.",
                "orcid": "0000-0003-3560-355X",
                "clpid": "Hyster-Todd-K"
            },
            {
                "family_name": "Farwell",
                "given_name": "Christopher C.",
                "clpid": "Farwell-Christopher-C"
            },
            {
                "family_name": "Huang",
                "given_name": "Audrey",
                "clpid": "Huang-Audrey-N"
            },
            {
                "family_name": "Arnold",
                "given_name": "Frances H.",
                "orcid": "0000-0002-4027-364X",
                "clpid": "Arnold-F-H"
            }
        ],
        "abstract": "Sigmatropic rearrangements, while rare in biology, offer opportunities for the efficient and selective synthesis of complex chemical motifs. A \"P411\" serine-ligated variant of cytochrome P450_(BM3) has been engineered to initiate a sulfimidation/[2,3]-sigmatropic rearrangement sequence in whole E. coli cells, a non-natural function for any enzyme, providing access to enantioenriched, protected allylic amines. Five mutations in the enzyme substantially enhance its activity toward this new function, demonstrating the evolvability of the catalyst toward challenging nitrene transfer reactions. The evolved catalyst additionally performs the highly enantioselective imidation of non-allylic sulfides.",
        "doi": "10.1002/anie.201601056",
        "pmcid": "PMC4818679",
        "issn": "1433-7851",
        "publisher": "Wiley",
        "publication": "Angewandte Chemie International Edition",
        "publication_date": "2016-04-04",
        "series_number": "15",
        "volume": "55",
        "issue": "15",
        "pages": "4711-4715"
    },
    {
        "id": "authors:0zwvs-azt80",
        "collection": "authors",
        "collection_id": "0zwvs-azt80",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20150504-091714076",
        "type": "article",
        "title": "Enantioselective Enzyme-Catalyzed Aziridination Enabled by Active-Site Evolution of a Cytochrome P450",
        "author": [
            {
                "family_name": "Farwell",
                "given_name": "Christopher C.",
                "clpid": "Farwell-Christopher-C"
            },
            {
                "family_name": "Zhang",
                "given_name": "Ruijie K.",
                "orcid": "0000-0002-7251-5527",
                "clpid": "Zhang-Ruijie-K"
            },
            {
                "family_name": "McIntosh",
                "given_name": "John A.",
                "orcid": "0000-0002-9487-490X",
                "clpid": "McIntosh-John-A"
            },
            {
                "family_name": "Hyster",
                "given_name": "Todd K.",
                "orcid": "0000-0003-3560-355X",
                "clpid": "Hyster-Todd-K"
            },
            {
                "family_name": "Arnold",
                "given_name": "Frances H.",
                "orcid": "0000-0002-4027-364X",
                "clpid": "Arnold-F-H"
            }
        ],
        "abstract": "One of the greatest challenges in protein design is creating new enzymes, something evolution does all the time, starting from existing ones. Borrowing from nature's evolutionary strategy, we have engineered a bacterial cytochrome P450 to catalyze highly enantioselective intermolecular aziridination, a synthetically useful reaction that has no natural biological counterpart. The new enzyme is fully genetically encoded, functions in vitro or in whole cells, and can be optimized rapidly to exhibit high enantioselectivity (up to 99% ee) and productivity (up to 1,000 catalytic turnovers) for intermolecular aziridination, demonstrated here with tosyl azide and substituted styrenes. This new aziridination activity highlights the remarkable ability of a natural enzyme to adapt and take on new functions. Once discovered in an evolvable enzyme, this non-natural activity was improved and its selectivity tuned through an evolutionary process of accumulating beneficial mutations.",
        "doi": "10.1021/acscentsci.5b00056",
        "pmcid": "PMC4571169",
        "issn": "2374-7951",
        "publisher": "American Chemical Society",
        "publication": "ACS Central Science",
        "publication_date": "2015-05-27",
        "series_number": "2",
        "volume": "1",
        "issue": "2",
        "pages": "89-93"
    }
]