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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Cofactors and Coenzymes01:27

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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Related Experiment Video

Updated: Jul 16, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Tuning Multistep Biocatalysis through Enzyme and Cofactor Colocalization in Charged Porous Protein Macromolecular

Yang Wang1, Trevor Douglas1

  • 1Department of Chemistry, Indiana University, 800 E Kirkwood Avenue, Bloomington, Indiana 47405, United States.

ACS Applied Materials & Interfaces
|September 11, 2023
PubMed
Summary

Researchers created a synthetic material that enhances enzyme efficiency by controlling cofactor localization and mobility. This bioinspired scaffold improves multistep biocatalysis, offering a 5-fold increase in efficiency by mimicking natural metabolic organization.

Keywords:
biocatalysiscascade reactioncollective behaviorfunctional materialheterogeneous catalystprotein macromolecular frameworksubstrate channelingvirus-like particle

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Materials Science and Nanotechnology
  • Synthetic Biology

Background:

  • Spatial organization of enzymes is vital for efficient metabolism in organisms.
  • Artificial scaffolds can host coupled enzymes for acellular multistep reactions.
  • Substrate channeling is challenging in vitro due to intermediate diffusion.

Purpose of the Study:

  • To investigate cofactor-enzyme colocalization in a synthetic bioinspired material.
  • To modulate multistep biocatalysis by controlling nicotinamide adenine dinucleotide (NAD) localization and diffusion.
  • To understand the impact of ionic strength on enzyme cascade efficiency.

Main Methods:

  • Formation of a protein macromolecular framework (PMF) from P22 virus-like particles (VLPs).
  • Covalent attachment of enzymes to the VLP exterior within the PMF.
  • Electrostatic partitioning of NAD conjugated to a polycationic species into the PMF.
  • Modulation of ionic strength to tune PMF-NAD interactions and enzyme efficiency.

Main Results:

  • Effective control of NAD localization and diffusion within the PMF, enabling substrate channeling.
  • Ionic strength modulation oppositely affected cofactor partitioning and mobility.
  • Observed up to a 5-fold increase or 75% decrease in multistep efficiency compared to free enzymes.

Conclusions:

  • Colocalization and mobility of cofactors are critical for multistep biocatalysis efficiency.
  • Hierarchical bioassemblies can be used to construct functional materials for tunable enzyme cascades.
  • This approach offers a strategy for designing efficient and cost-effective acellular biocatalytic systems.