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Showing 1–14 of 14 results
Advanced filters: Author: Rey-Ting Guo Clear advanced filters

  • Poly-ethylene terephthalate (PET) is a widely used plastic which accumulates in the environment with detrimental consequences. Here the authors report crystal structures of a PET-hydrolyzing enzyme from the microbe Ideonella sakaiensis bound to substrate and product analogs, and suggest a catalytic mechanism for its PET-degrading activity.

    • Xu Han
    • Weidong Liu
    • Rey-Ting Guo
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-6

  • 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

  • BcABA3 catalyzes farnesyl pyrophosphate cyclization but lacks features to be recognized as a terpene cyclase. Here, authors report crystal structures of BcABA3 and homologues to reveal the molecular basis of this distinct type of enzyme.

    • Siyu Li
    • Jian-Wen Huang
    • Rey-Ting Guo
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-8

  • 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

  • Bio-degradation of poly(butylene adipate-co-terephthalate) is an attractive tactic but requires an effective hydrolytic enzyme. Here, the authors demonstrate that cutinases are highly potent PBAT-decomposing enzymes and their mechanism is proposed based on substrate-binding mode.

    • Yu Yang
    • Jian Min
    • Rey-Ting Guo
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-8

  • In the face of global plastic pollution, enzymatic degradation of poly(ethylene terephthalate) (PET) has attracted much attention. Now, structural and biochemical studies reveal a minimal mutational strategy to increase the activity of PET-degrading enzymes, with potential evolutionary implications.

    • Chun-Chi Chen
    • Xu Han
    • Rey-Ting Guo
    Research
    Nature Catalysis
    Volume: 4, P: 425-430

  • Phosphoantigen-mediated BTN2A1 association drives BTN3A1 intracellular fluctuations outwards in a thermodynamically favourable manner, thereby enabling BTN3A1 to push off from the BTN2A1 ectodomain to initiate T cell receptor–mediated γδ T cell activation.

    • Linjie Yuan
    • Xianqiang Ma
    • Yonghui Zhang
    ResearchOpen Access
    Nature
    Volume: 621, P: 840-848

  • The nitrile synthase AetD is a crucial component in the biosynthetic pathway of neurotoxin aetokthonotoxin (AETX). Here, the authors solved crystal structures of AetD in complex with different substrates, revealing that AetD represents a new type of HO-like diiron enzyme and the possibility of expanding its substrate spectrum.

    • Hao Li
    • Jian-Wen Huang
    • Chun-Chi Chen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-9

  • Self-sufficient cytochrome P450 monooxygenases, which contain all redox partners in a single polypeptide chain, are of interest for biotechnological applications. Here, the authors present the crystal structure of full-length Thermobispora bispora CYP116B46 and discuss the potential electron transfer pathway.

    • Lilan Zhang
    • Zhenzhen Xie
    • Chun-Chi Chen
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-6

  • Reductive desymmetrization of 2,2-disubstituted cyclodiketones can provide valuable complex molecules with multiple chiral centres, but the generation of a single stereoisomer is difficult. This work addresses this synthetic challenge by engineering the activity and stereoselectivity of a carbonyl reductase.

    • Xi Chen
    • Hongliu Zhang
    • Yanhe Ma
    Research
    Nature Catalysis
    Volume: 2, P: 931-941

  • Diterpene synthase VenA catalyses the synthesis of venezuelaene A with a unique 5-5-6-7 tetracyclic skeleton from geranylgeranyl pyrophosphate. Here, the authors report crystal structures of apo- and holo-VenA, provide mechanistic insights into its substrate selectivity and promiscuity, and engineer VenA into a sesterterpene synthase.

    • Zhong Li
    • Lilan Zhang
    • Shengying Li
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • Microorganisms enzymatically degrade natural polymers and synthetic plastics to enable a sustainable environment. This Review describes common features of these enzymes and how they can be harnessed to convert waste into useful precursors.

    • Chun-Chi Chen
    • Longhai Dai
    • Rey-Ting Guo
    Reviews
    Nature Reviews Chemistry
    Volume: 4, P: 114-126