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Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...

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Nanosensors to Detect Protease Activity In Vivo for Noninvasive Diagnostics

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Published on: July 16, 2018

A Nanopore Sensing Assay Resolves Cascade Reactions in a Multienzyme System.

Yingying Sheng^1,2, Ke Zhou¹, Lei Liu³

¹Beijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences, Beijing, 100190, China.

Angewandte Chemie (International Ed. in English)

|March 3, 2022

Summary

This study introduces a nanopore sensing assay to quantify intermediates in enzymatic cascade reactions. The method reveals substrate channeling in confined environments, aiding multienzyme system design.

Keywords:

Cascade Reactions Multienzyme Systems Nanopore Sensing Substrate Channelling

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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Area of Science:

Biochemistry
Nanotechnology
Synthetic Biology

Background:

Enzymatic cascade reactions synthesize complex molecules using sequential enzyme steps.
Substrate channeling, where intermediates are confined, is key to cascade efficiency.
Quantifying intermediates and channeling effects in artificial systems remains challenging.

Purpose of the Study:

To develop a nanopore sensing assay for quantifying reaction intermediates and products in a three-enzyme system.
To investigate substrate channeling in both solution and confined environments (liposomes).
To provide a tool for evaluating and designing artificial multienzyme systems.

Main Methods:

Utilized a DNA-peptide complex as a substrate for sequential enzymatic cleavage.
Employed nanopore translocation recordings to monitor temporal changes of intermediates and product.
Compared enzyme behavior in bulk solution versus within liposomes.

Main Results:

Successfully quantified all intermediates and the final product of the artificial three-enzyme system.
Demonstrated that substrate channeling occurs between specific enzyme sets within liposomes.
Observed differences in reaction dynamics between solution and confined environments.

Conclusions:

The developed nanopore assay accurately quantifies cascade reaction components.
Substrate channeling is confirmed and influenced by confinement in multienzyme systems.
This approach offers a powerful method for designing and assessing artificial enzymatic systems.