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Related Concept Videos

Enzymes02:34

Enzymes

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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.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Enzyme Kinetics01:19

Enzyme Kinetics

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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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Enzyme Inhibition01:30

Enzyme Inhibition

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Introduction to Enzymes01:22

Introduction to Enzymes

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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
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Restriction Enzymes01:11

Restriction Enzymes

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
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Related Experiment Video

Updated: Jan 28, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

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Protein-based scaffolds for enzyme immobilization.

Guoqiang Zhang1, Sarah Schmidt-Dannert1, Maureen B Quin1

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, United States.

Methods in Enzymology
|February 21, 2019
PubMed
Summary

Protein scaffolds offer a robust method for immobilizing enzymes in biocatalytic cascades. This approach enhances efficiency and cost-effectiveness in synthesizing complex molecules.

Keywords:
BiocatalysisEnzyme cascadeImmobilizationProtein scaffoldSelf-assembling

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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Protein Engineering and Synthetic Biology
  • Chemical Synthesis and Process Development

Background:

  • Biocatalysis presents a sustainable alternative to traditional chemical synthesis for complex molecules.
  • Efficient biocatalytic reaction cascades require robust, cost-effective, and self-sufficient enzyme systems.
  • Enzyme immobilization on solid supports enhances stability and optimizes reaction conditions.

Purpose of the Study:

  • To describe methods for designing and producing self-assembling protein scaffolds for enzyme coimmobilization.
  • To detail the characterization of protein scaffolds and the loading of biocatalytic enzymes.
  • To present approaches for testing the activity of immobilized biocatalytic cascades.

Main Methods:

  • Design and genetic encoding of self-assembling protein scaffolds.
  • In vitro coimmobilization of biocatalytic cascade enzymes onto protein scaffolds.
  • Characterization of scaffold properties and enzyme activity assays.
  • Development of a toolbox of scaffold building blocks with varied surface properties.

Main Results:

  • Demonstrated successful design and production of self-assembling protein scaffolds.
  • Validated methods for enzyme loading and activity assessment of immobilized cascades.
  • Established a versatile toolbox for adapting scaffolds to diverse biocatalysts and microenvironments.

Conclusions:

  • Self-assembling protein scaffolds provide an effective platform for organizing and immobilizing biocatalytic cascades.
  • This approach enhances the efficiency, robustness, and adaptability of biocatalysis for industrial applications.
  • The developed scaffold system and toolbox offer a flexible solution for optimizing biocatalytic processes.