Classification of Enzymes

Enzymes

Enzymes are nitrogenous organic molecules produced by living organisms such as plants and animals. A long chain of one or more amino acids is connected together using amide or peptide bonds to make them....

Structure of Enzyme

Enzymes are proteins that are made up of several polypeptide chains, also known as amino acids, that have been folded and coiled numerous times. They have linear chains of amino acids in three-dimensional structures. The enzyme’s catalytic activity is determined by the amino acid sequence. Only a small portion of an enzyme’s structure participates in catalysis and is located around the binding sites. They have separate sites; the active site of an enzyme is made up of the catalytic and binding sites....

Classification of Enzymes

The International Union of Biochemists divides enzymes into six types based on the sort of reaction they catalyse (I U B). Oxidoreductases, transferases, hydrolases, lyases, ligases, and isomerases are the six types of enzymes. The following are their functions:...

Enzyme Cofactor

Cofactors are chemical substances that are not proteins and are found in enzymes. A cofactor affects the action of an enzyme by acting as a catalyst. Apoenzymes are enzymes that do not require a cofactor. The holoenzyme is made up of an enzyme and its cofactor....

Mechanism of Enzyme Action

The active site of an enzyme draws substrates and catalyses the chemical process that produces products. Allows the products to disassociate or detach from the enzyme’s surface after product production. The enzyme-substrate complex is the combination of an enzyme and its substrates....

Enzymes as Biochemical Catalysts

Biochemical catalysts are also known as enzymes, and the phenomenon is known as biochemical catalysis. Enzymes are widely used to enhance or expedite the efficient preparation and effect of beverages, chocolates, curd, predigested infant food, washing powders, and other products....

Examples of Enzyme Catalysis

Cane sugar inversion: Cane sugar is converted to glucose and fructose by the enzyme invertase....

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....

Drug Action of Enzymes

Drugs that act on the active sites of enzymes can control, i.e. inhibit or stimulate, enzyme function. The majority of medications that act on enzymes are inhibitors, and the majority of them are competitive inhibitors, meaning they compete with the enzyme’s substrate for binding. The bulk of the original (first generation) kinase inhibitors, for example, bind to the enzyme’s ATP pocket....

Examples of Enzymes

Lipases are a group of enzymes that aid in the digestion of lipids in the intestine. Amylase is a protein that aids in the conversion of carbohydrates to sugars. Saliva contains this enzyme. Maltase is a sugar that breaks down maltose into glucose and is found in saliva. Maltose can be found in a variety of foods, including potatoes, pasta, and beer. Trypsin is an enzyme that breaks down proteins into amino acids and is located in the small intestine. Lactase is an enzyme present in the small intestine that aids in the breakdown of lactose, a sugar found in milk, into glucose and galactose. Helicase is a DNA unravelling enzyme. DNA Polymerase is a type of enzyme that makes DNA from deoxyribonucleotides....

Chemical Nature of Enzyme

Enzymes are primarily composed of proteins. Proteins are made up of chains of amino acids. Amino acids are folded into specific three-dimensional shapes, determining the enzyme’s structure. The structure includes an active site where the substrate binds and catalytic reactions occur. Enzymes can also be RNA molecules, although less common than protein enzymes. The sequence and structure of amino acids in enzymes dictate their function and specificity for particular substrates....

Enzymes – FAQs

What is the function of all enzymes?...