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Enzyme Inhibition

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.

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...

Introduction to Mechanisms of Enzyme Catalysis

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Enzymes

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Updated: May 20, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Control of enzyme-solid interactions via chemical modification.

Ruma Chowdhury¹, Bobbi Stromer, Binod Pokharel

¹Department of Chemistry, University of Connecticut, U-3060, Storrs, Connecticut 06269, USA.

Langmuir : the ACS Journal of Surfaces and Colloids

|July 24, 2012

Summary

Enzyme cationization enhances binding affinity to solid surfaces by modifying surface charges. This chemical strategy significantly boosts enzyme-solid interactions while preserving biocatalytic activity.

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Area of Science:

Biochemistry
Materials Science
Surface Chemistry

Background:

Electrostatic forces play a crucial role in enzyme-solid interactions.
Controlling these interactions for high-affinity, benign enzyme adsorption on solids is challenging.
Surface charge modification offers a potential strategy to modulate enzyme-surface binding.

Purpose of the Study:

To investigate the effect of enzyme cationization on binding affinities to solid surfaces.
To demonstrate a chemical method for adjusting enzyme net charge and controlling adsorption.
To assess the impact of cationization on enzyme structure and activity retention.

Main Methods:

Chemical modification of surface carboxyl groups on enzymes using tetraethylenepentamine (TEPA) to create cationized proteins.
Utilizing negatively charged nanosolid, α-Zr(HPO(4))(2)·H(2)O (α-ZrP), as a model surface.
Assessing binding affinities, structural integrity (circular dichroism), and enzymatic activities of modified and unmodified enzymes.

Main Results:

Cationized glucose oxidase (GO) exhibited a 250-fold increase in affinity for α-ZrP compared to unmodified GO.
Cationized methemoglobin (Hb) showed a 26-fold increase in affinity for α-ZrP.
Cationized enzymes retained significant structural integrity and considerable biocatalytic activity post-modification and binding.

Conclusions:

Enzyme cationization is an effective strategy to enhance enzyme-solid binding affinities by 1-2 orders of magnitude.
This chemical modification approach allows for rational control over enzyme-surface interactions.
The method preserves substantial biocatalytic properties of enzymes, offering a powerful tool for biomaterial design.