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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...

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Related Experiment Video

Updated: Dec 29, 2025

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Nonspherical Coacervate Shapes in an Enzyme-Driven Active System.

Willem Kasper Spoelstra¹, Eli O van der Sluis¹, Marileen Dogterom¹

¹Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2628 CJ Delft, The Netherlands.

Langmuir : the ACS Journal of Surfaces and Colloids

|January 30, 2020

Summary

Enzymatically active RNA coacervates exhibit transient nonspherical shapes. Their morphology is influenced by enzyme concentration and temperature, with enzymatic activity potentially leading to coacervate degradation.

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Area of Science:

Biochemistry
Polymer Science
Cell Biology

Background:

Coacervates are polymer-rich droplets formed via liquid-liquid phase separation.
Coacervation is increasingly recognized for its role in organizing biological systems.
The impact of enzymatic and chemical reactions on coacervation dynamics remains poorly understood.

Purpose of the Study:

To investigate the influence of enzymatic activity on coacervate formation and morphology.
To characterize a model system of RNA coacervates with active RNA polymerase.
To explore the relationship between biochemical processes and coacervate behavior.

Main Methods:

Formation and characterization of coacervates containing spermine, RNA, nucleotides, and PNPase.
Systematic variation of PNPase concentration, UDP concentration, and temperature.
Microscopy and biochemical assays to analyze coacervate shape, enzyme localization, and activity.

Main Results:

Enzymatically active RNA coacervates display transient nonspherical shapes.
Coacervate morphology is significantly affected by PNPase concentration, UDP levels, and temperature.
PNPase localizes within the coacervate phase, and its depolymerization activity can degrade the coacervates.

Conclusions:

Biochemical activity, specifically enzymatic depolymerization, can dynamically alter coacervate structure.
Nonspherical coacervate shapes may be a consequence of internal biochemical processes.
These findings suggest a link between (bio)chemical activity and the functional biology of coacervates.