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Showing 1–4 of 4 results
Advanced filters: Author: Chengsen Cui Clear advanced filters

  • The Duf4243 dioxygenases GedK and BTG13 are known to catalyze the aromatic cleavage of bulky tricyclic hydroquinone. Here, the authors discover a distinct Duf4243 dioxygenase PaD that favors small monocyclic hydroquinones from the penicillic-acid biosynthetic pathway and determine the structural basis for its changed substrate specificity.

    • Chengsen Cui
    • Lu-Jia Yang
    • Shu-Shan Gao
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-10

  • The unique structure and mechanism of chanoclavine synthase (EasC), a haem catalase that uses superoxide for substrate transformation in ergot alkaloid biosynthesis, are revealed in this study, challenging established catalase mechanisms.

    • Chun-Chi Chen
    • Zhi-Pu Yu
    • Shu-Shan Gao
    ResearchOpen Access
    Nature
    Volume: 640, P: 840-846

  • Chiral heterocyclic compounds are privileged structures in medicinal chemistry. Here, the authors report an in silico strategy for the enzymatic synthesis of pharmaceutically significant chiral N- and O-heterocycles via Baldwin cyclization of hydroxy- and amino-substituted epoxides and oxetanes using epoxide hydrolase mutants.

    • Jun-Kuan Li
    • Ge Qu
    • Zhoutong Sun
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • Imine reductases can catalyze reductive amination reactions to produce chiral amines, however, transformation of bulky amines has been challenging. Here, by using an increasing-molecule-volume-screening method, the authors identify a group of imine reductases that can accept bulky amines and achieve an efficient gram-scale synthesis of an API sensipar analogue.

    • Jun Zhang
    • Xin Li
    • Chengsen Cui
    ResearchOpen Access
    Communications Chemistry
    Volume: 5, P: 1-9