Substrate-Induced Self-Assembly of Cooperative Catalysts

Pablo Solís Muñana1, Giulio Ragazzon2, Julien Dupont1

  • 1School of Sciences Auckland University of Technology Private Bag 92006 Auckland 1142 New Zealand.

Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)
|April 22, 2020
PubMed
Summary

Researchers created a synthetic system where a substrate drives the formation of vesicular assemblies. These assemblies then cooperatively catalyze the cleavage of the same substrate, mimicking natural dissipative self-assembly.

Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

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...
10.3K
Catalysis02:50

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
29.9K
Enzymes02:34

Enzymes

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...
92.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
8.5K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.9K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K