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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 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...

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...

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.

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Related Experiment Video

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Design of Solid-State Fermentation Systems for Polymer Hydrolytic Extracellular Enzyme Production by Filamentous Fungi

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[Structure-function relationships of industrial enzymes].

Kun Zhang¹, Ge Qu¹, Weidong Liu¹

¹Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology

|November 1, 2019

Summary

This summary is machine-generated.

Industrial enzymes are crucial for bio-industries. Understanding enzyme structure-function relationships enables rational and de novo design for advanced applications.

Keywords:

biocatalysis industrial enzymes structural flexibility structure-function

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Area of Science:

Biotechnology
Enzymology
Protein Engineering

Background:

Industrial enzymes are vital components driving the bio-industry and its downstream sectors.
Understanding the link between enzyme structure and function is essential for optimizing industrial applications.

Purpose of the Study:

To review advancements in studying industrial enzyme structure-function relationships.
To highlight the applications of this knowledge in enzyme design and development.

Main Methods:

Review of protein crystallization techniques.
Analysis of computational simulation methodologies.
Synthesis of current research on enzyme structure-function correlations.

Main Results:

Advanced technologies facilitate detailed studies of enzyme structure-function relationships.
Rational and de novo enzyme design are becoming feasible.
Significant progress has been made in understanding and applying these relationships.

Conclusions:

Continued research into enzyme structure-function is key for innovation.
Future developments will likely focus on enhanced enzyme design and novel applications.