Factors Affecting Enzyme Catalysis
- Concentration of Substrate: In the presence of an enzyme, the rate of a chemical reaction increases as the substrate concentration rises until a limiting rate is achieved, after which additional increases in the substrate concentration have no effect on the reaction. The enzyme molecules are saturated with the substrate at this point. The extra substrate molecules are unable to react until the substrate that has already been bound to the enzymes has reacted and been released.
- Concentration of Enzyme: When the enzyme concentration is much lower than the substrate concentration, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. This is true for any catalyst; when the catalyst concentration rises, the reaction rate rises as well.
- Temperature: For most chemical reactions, a temperature increase of 10°C about doubles the reaction rate, according to a well-known rule of thumb. This rule applies to all enzymatic reactions to some extent. Even a slight increase in temperature, after a certain threshold, induces denaturation of the protein structure and disruption of the active site, resulting in a drop in reaction rate.
- Hydrogen Ion Concentration (pH): Most enzymes are proteins, and they are sensitive to variations in pH or hydrogen ion concentration. The degree of ionisation of an enzyme’s acidic and basic side groups, as well as the substrate components, is affected by changes in pH. The catalytic activity of an enzyme is altered when one of these charges is neutralised. Over a narrow pH range, an enzyme’s activity is at its peak. The enzyme’s optimal pH is determined by the median value of this pH range.
- Inhibition of Enzymes: Enzymes must occasionally be slowed to aid and ensure that our bodies’ systems operate appropriately and efficiently. For example, if an enzyme produces too much of a product, it must be possible to reduce or stop production. Inhibitors are required in such situations.
Enzymes Inhibition: A molecule blocks the active site, causing the substrate to compete with the inhibitor for binding to the enzyme. Non-competitive inhibitors bind to an enzyme in a location other than the active site, reducing its effectiveness. Inhibitors that bind to the enzyme-substrate complex are known as noncompetitive inhibitors. The products exit the active site with less ease, slowing the reaction. Irreversible inhibitors bind to an enzyme and render it inactive for the rest of its life.
Enzymes – Definition, Structure, Classification, Examples
Enzymes are biological molecules that act as catalysts, speeding up chemical responses in living organisms. They work by lowering the activation energy needed for a response to do, therefore adding the rate of the response without being consumed themselves. Enzymes play pivotal places in colorful natural processes, similar as metabolism, digestion, and cell signaling.
Table of Content
- Enzymes
- Structure of Enzyme
- Classification of Enzymes
- Enzyme Cofactor
- Mechanism of Enzyme Action
- Enzymes as Biochemical Catalysts
- Examples of Enzyme Catalysis
- Factors Affecting Enzyme Catalysis
- Drug Action of Enzymes
- Examples of Enzymes
- Chemical Nature of Enzyme