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  • Title: [Advances in the structure and function of MHETase].
    Author: Yang M, Fan F, He L, Chen J, Wang L, Qiu S, Lyu C, Huang J.
    Journal: Sheng Wu Gong Cheng Xue Bao; 2024 Sep 25; 40(9):2812-2830. PubMed ID: 39319709.
    Abstract:
    Polyethylene terephthalate (PET) is one of the widely used plastics, but its waste pollution has become a global environmental issue. The discovery of polyethylene terephthalate hydrolase (PETase) has provided a green and environmentally friendly approach for PET degradation. However, PETase produces intermediate products that inhibit the enzyme's further activity, leading to a decrease in enzyme efficiency. Mono(2-hydroxyethyl) terephthalate hydrolase (MHETase) works synergistically with PETase to further degrade the intermediate product MHET into ethylene glycol (EG) and terephthalic acid (TPA). MHETase exhibits extremely high specificity for MHET and is crucial for the complete degradation of PET. This article comprehensively reviews MHETase from various perspectives, including its three-dimensional structure, substrate binding, and catalytic mechanism. It demonstrates the structural features and key residues associated with the enzyme's degrading activity and discusses the progress in enzyme engineering modifications. Additionally, the study envisions the development of a two-enzyme PET degradation system by combining MHETase with PETase, aiming to provide valuable references for designing and developing more efficient PET hydrolytic enzyme systems.
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