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Showing 1–6 of 6 results
Advanced filters: Author: Sean A. Newmister Clear advanced filters

  • Biocatalysis of the chemotherapy drug, doxorubicin, relies on the cytochrome P450 DoxA, which is inefficient. Here, the authors ameliorated the biosynthetic limitations by identifying DoxA redox partners and DnrV, which prevents product inhibition, helping improve microbial production.

    • Arina Koroleva
    • Erika Artukka
    • Mikko Metsä-Ketelä
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-13

  • The complete biosynthesis of the fungal indole alkaloid malbrancheamide, which culminates in an intramolecular [4+2] hetero-Diels–Alder cyclization to produce the bicyclo[2.2.2]diazaoctane scaffold, has now been discovered. Chemical synthesis and protein structural analysis were used to provide mechanistic insight into this enzyme-dependent diastereo- and enantioselective cycloaddition.

    • Qingyun Dan
    • Sean A. Newmister
    • Robert M. Williams
    Research
    Nature Chemistry
    Volume: 11, P: 972-980

  • A Diels–Alderase that catalyses the inherently disfavoured cycloaddition and forms a bicyclo[2.2.2]diazaoctane scaffold with a strict α-anti-selectivity has now been discovered. This Diels–Alderase, called CtdP, is an NmrA-like protein. Isotopic labelling, structural biology and computational studies reveal that the CtdP-catalysed Diels–Alder reaction involves a NADP+/NADPH-dependent redox mechanism.

    • Zhiwen Liu
    • Sebastian Rivera
    • Xue Gao
    Research
    Nature Chemistry
    Volume: 15, P: 526-534

  • Characterization of a family of Stigonematales (Stig) cyclases that catalyze stereoselective intramolecular C–C bond formation reveals the enzymatic origins of the complex stereochemical patterns in hapalindole and fischerindole alkaloids.

    • Shasha Li
    • Andrew N Lowell
    • David H Sherman
    Research
    Nature Chemical Biology
    Volume: 13, P: 467-469

  • The biogenesis and stereochemical origin of many natural products remain unknown. Now the biosynthetic pathway of brevianamide A is elucidated. An isomerase is discovered that can catalyse pinacol rearrangement without a cofactor and determine the stereochemistry of the bicyclo[2.2.2]diazaoctane ring.

    • Ying Ye
    • Lei Du
    • Shengying Li
    Research
    Nature Catalysis
    Volume: 3, P: 497-506

  • The structure of a Stig cyclase, HpiC1, reveals how it catalyzes Cope rearrangement and 6-exo-trig cyclization, including how it controls the position of electrophilic aromatic substation that distinguishes hapalindole from fischerindole alkaloids.

    • Sean A. Newmister
    • Shasha Li
    • David H. Sherman
    Research
    Nature Chemical Biology
    Volume: 14, P: 345-351