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Enzymes

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...

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...

Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

Most enzymes...

Induced-fit Model

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...

Introduction to Enzyme Kinetics

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...

Introduction to Enzymes

Introduction to Enzymes

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.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...

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Related Experiment Video

Updated: May 16, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Designing Enzymatic Reactivity with an Expanded Palette.

Reuben B Leveson-Gower¹

¹Biocatalysis Section, Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629HZ, Delft, The Netherlands.

Chembiochem : a European Journal of Chemical Biology

|April 4, 2025

Summary

Enzymes are limited in the reactions they can catalyze. Researchers are expanding biocatalysis by incorporating noncanonical amino acids and synthetic cofactors, enabling new chemical reactions for sustainable synthesis.

Keywords:

biocatalysis directed evolution noncanonical amino acids photobiocatalysis unnatural cofactors

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Last Updated: May 16, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

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Published on: August 8, 2016

Area of Science:

Biochemistry
Organic Chemistry
Sustainable Chemistry

Background:

Biocatalysis offers a greener alternative for chemical and pharmaceutical industries.
Current enzymatic reactions cover only a fraction of needed synthetic routes.
Canonical amino acids and cofactors limit enzyme catalytic potential.

Purpose of the Study:

To review recent advancements in expanding biocatalytic reactivity.
To highlight the use of noncanonical components in enzyme engineering.
To provide an outlook on future directions for biocatalysis.

Main Methods:

Incorporation of noncanonical amino acids into enzyme structures.
Design and use of synthetic cofactors for novel enzymatic functions.
Synergistic use of exogenous photocatalysts with natural enzymes.

Main Results:

Enabled new enzymatic reactions via organocatalytic, organometallic, and photocatalytic mechanisms.
Diverted natural enzyme reactivity towards radical pathways using photocatalysts.
Demonstrated expanded catalytic possibilities beyond natural enzyme limitations.

Conclusions:

Enriching enzymatic chemistry with unnatural components significantly broadens biocatalytic applications.
Future developments are needed to enhance practicality and sustainability in biocatalysis.
Expanding the enzyme design palette is crucial for greener chemical synthesis.