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    Non-native Metabolon-based Bioelectrocatalytic System Using Chimeric Invertase-Glucose Dehydrogenase = 인버타제-포도당탈수소효소 키메라를 활용한 비자연계 메타볼론 기반 전기촉매 시스템

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    https://www.riss.kr/link?id=T17329896

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    Enzymes are well recognized as very potent biocatalysts in the natural world, exerting a substantial
    influence on several metabolic processes. Enzymes often exist in a state that might potentially exhibit increased
    reaction efficiency inside the biological system via the formation of a multienzyme complex. In the present
    work, an in vitro system was developed by constructing a non-native metabolon by the deliberate conjugation
    of two enzymes originating from distinct sources. In this study, we have discovered the key parameters that
    have the potential to significantly impact the efficiency of the reaction. Glucose dehydrogenase (GDHαγ) was
    chosen as a representative enzyme due to its established credibility and extensively verified characteristics in
    prior studies. The coupling enzyme used for this study was invertase (INV), which has the ability to create
    glucose as an intermediate. In order to merge the two enzymes, a peptide spacer was used as a connecting
    element between GDHαγ and INV. The catalytic activity was significantly impacted by the expression order of
    GDHαγ and INV, and the catalytic activity exhibited notable variations based on the spacer sequence. The
    criticality of regulating the distance and orientation between the coupling enzymes in a cascade reaction has
    been identified.
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    Enzymes are well recognized as very potent biocatalysts in the natural world, exerting a substantial influence on several metabolic processes. Enzymes often exist in a state that might potentially exhibit increased reaction efficiency inside the bio...

    Enzymes are well recognized as very potent biocatalysts in the natural world, exerting a substantial
    influence on several metabolic processes. Enzymes often exist in a state that might potentially exhibit increased
    reaction efficiency inside the biological system via the formation of a multienzyme complex. In the present
    work, an in vitro system was developed by constructing a non-native metabolon by the deliberate conjugation
    of two enzymes originating from distinct sources. In this study, we have discovered the key parameters that
    have the potential to significantly impact the efficiency of the reaction. Glucose dehydrogenase (GDHαγ) was
    chosen as a representative enzyme due to its established credibility and extensively verified characteristics in
    prior studies. The coupling enzyme used for this study was invertase (INV), which has the ability to create
    glucose as an intermediate. In order to merge the two enzymes, a peptide spacer was used as a connecting
    element between GDHαγ and INV. The catalytic activity was significantly impacted by the expression order of
    GDHαγ and INV, and the catalytic activity exhibited notable variations based on the spacer sequence. The
    criticality of regulating the distance and orientation between the coupling enzymes in a cascade reaction has
    been identified.

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