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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Regulation of Metabolism01:19

Regulation of Metabolism

Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
Enzyme Inhibition01:30

Enzyme Inhibition

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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Related Experiment Video

Updated: Jun 24, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Controlling protein retention on enzyme-responsive surfaces.

Rachel E Rawsterne1, Julie E Gough, Frank J M Rutten

  • 1School of Materials, The University of Manchester, Grosvenor Street, Manchester, M1 7HS, UK.

Surface and Interface Analysis : SIA
|March 28, 2009
PubMed
Summary

Researchers developed enzyme-triggered surfaces by selectively cleaving peptides with proteases. This method offers controllable surface property changes, overcoming challenges in enzyme retention for advanced material applications.

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

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Last Updated: Jun 24, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Area of Science:

  • Materials Science
  • Biochemistry
  • Surface Chemistry

Background:

  • Surface property modification is crucial for many technologies.
  • Existing methods use physical or chemical stimuli.
  • Enzyme-catalyzed changes offer a novel approach to surface manipulation.

Purpose of the Study:

  • To develop surfaces with properties that can be altered by enzyme catalysis.
  • To demonstrate selective peptide hydrolysis on surfaces using proteases.
  • To address challenges related to enzyme retention on surfaces.

Main Methods:

  • Synthesizing surface-tethered fluorenylmethoxycarbonyl-dipeptides.
  • Utilizing alpha-chymotrypsin and thermolysin for peptide hydrolysis.
  • Employing ToF-SIMS and XPS for surface analysis.
  • Investigating PEG(200) adsorption to improve enzyme retention.

Main Results:

  • Selective cleavage of surface-tethered peptides by proteases was achieved.
  • Alpha-chymotrypsin was successfully deposited and retained on surfaces.
  • Thermolysin demonstrated selective peptide cleavage and was removable by washing.
  • PEG(200) adsorption was explored to manage enzyme retention.

Conclusions:

  • Enzyme-triggered surface modification is feasible using selective protease catalysis.
  • Surface analysis confirmed enzyme deposition, activity, and removal.
  • Strategies to manage enzyme-surface interactions are critical for controlled surface changes.