2016
DOI: 10.1038/srep39587
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Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex

Abstract: Multistep cascade reactions in nature maximize reaction efficiency by co-assembling related enzymes. Such organization facilitates the processing of intermediates by downstream enzymes. Previously, the studies on multienzyme nanocomplexes assembled on DNA scaffolds demonstrated that closer interenzyme distance enhances the overall reaction efficiency. However, it remains unknown how the active site orientation controlled at nanoscale can have an effect on multienzyme reaction. Here, we show that controlled ali… Show more

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Cited by 20 publications
(25 citation statements)
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“…An extensive review on loops and linkers elaborates on linker design in great detail and emphasizes how linkers are not merely “connectors”, but have an important effect on the microenvironment and orientation of the fusion . It turns out that the orientation between the two enzymes, as a consequence of the linker, can have a significant impact on the efficiency of the reaction, although, in practice, this is difficult to control . Some studies point out that by performing computational simulations and/or using linker databases, a more consistent and less arbitrary design can be established, as exemplified by the studies mentioned above, even though up to now this has hardly been integrated with enzyme fusions.…”
Section: Fusion Design and Linker Designmentioning
confidence: 99%
“…An extensive review on loops and linkers elaborates on linker design in great detail and emphasizes how linkers are not merely “connectors”, but have an important effect on the microenvironment and orientation of the fusion . It turns out that the orientation between the two enzymes, as a consequence of the linker, can have a significant impact on the efficiency of the reaction, although, in practice, this is difficult to control . Some studies point out that by performing computational simulations and/or using linker databases, a more consistent and less arbitrary design can be established, as exemplified by the studies mentioned above, even though up to now this has hardly been integrated with enzyme fusions.…”
Section: Fusion Design and Linker Designmentioning
confidence: 99%
“…Bifunctional DBCO derived linkers were used to conjugate both the enzymes via in strain-promoted azide–alkyne cycloaddition (SPAAC) and inverse electron demand Diels–Alder reaction (IEDDA). The d -mannitol production in two different orientations of the enzymes, (1) active sites facing each other (face to face, FF) conjugate and (2) active site oriented in the opposite direction (back to back, BB) conjugate, was 36.3 ± 7.7 μM and 21.9 ± 1.6 μM, respectively …”
Section: Nature-inspired Strategies To Assemble Multienzymes Togethermentioning
confidence: 99%
“…The possible mechanistic explanation behind the better efficacy of enzyme hydrogel can be answered by the orientation of the catalytic/active site of polyphenol oxidase in hydrogel network. Enhancement of activity of any immobilized oxidoreductive enzyme is dependent on the orientation of its active site that should be in such a fashion in immobilization network that provides proximity with its substrate and facilitates the catalysis [24]. Herein, the formation of the stable enzyme hydrogel resulted from the spontaneous interaction between hydrogel and PPO which in turn provided better catalysis of the said enzyme that is in soluble form (figure 11).…”
Section: Redox Activity Studymentioning
confidence: 99%