How Many Types of Enzymes are There

Introduction

• There are six types of Enzymes.

• The body produces enzymes, which are essentially proteins, to perform specific metabolic and biochemical reactions.

• They are biological catalysts that accelerate internal chemical reactions.

• Enzymes are necessary for several processes, including digestion and liver function.

• Like all catalysts, enzymes speed up reactions by reducing their activation energy or by providing an alternate pathway for the reaction. Some enzymes have the ability to accelerate substrate-to-product conversion by millions of times.

• Chemically speaking, enzymes are similar to any catalyst in that they are neither consumed by substances during chemical processes nor change the equilibrium of a reaction.

• The majority of other catalysts are not as selective as enzymes.

• On the Other hand, certain substances can influence the activity of an enzyme: activators and inhibitors both increase and reduce activity, respectively.

• Enzyme inhibitors are common medicinal medications and toxins.

• In addition, many enzymes are (permanently) denatured when exposed to extreme heat, losing their structure and catalytic characteristics. An enzyme's activity declines significantly outside of its ideal temperature and pH range.

Types of Enzymes

The corresponding enzymes are named after the six main types of metabolic reactions that take place in the body. They are:

1. Oxidoreductases

2. Transferases

3. Hydrolases

4. Lyases

5. Isomerases

6. ligases

Oxidoreductases:

These enzymes are known as oxidoreductases because they cause oxidation and reduction processes. These reactions involve the transfer of electrons in the form of hydrogen atoms or hydride ions. These enzymes serve as hydrogen donors when the oxidation of a substrate occurs. Dehydrogenases or reductases are the names of these enzymes. These enzymes are known as oxidases when the oxygen atom serves as the acceptor.

Transferases:

Transferring functional groups from one molecule to another is carried out by these enzymes. Alanine aminotransferase is an example of this, as it switches the alpha-amino group between alanine and aspartate, among other amino acids. Some transferases can also move phosphate groups from ATP to other molecules.

Hydrolases :

These enzymes support the hydrolysis process by catalysing reactions. They add water to dissolve single bonds. Some hydrolases break the peptide bonds in proteins, acting as digesting enzymes. Due to the fact that they move the water molecule from one substance to another, hydrolases might also be considered a form of transferase. Example: Glucose-6-phosphatase, which leaves just glucose and H3PO4 after removing the phosphate group from glucose-6-phosphate.

Lyases:

These enzymes catalyse the formation of double bonds via the removal of functional groups or the addition of functional groups to break double bonds in molecules. An illustration of a lyase is pyruvate decarboxylase, which takes CO2 out of pyruvate. Dehydratases and deaminases are more examples.

Isomerases:

These enzymes catalyse processes in which a functional group is transferred to a different location inside a single molecule, resulting in a new molecule that is actually an isomer of the original. For instance, glucose 6-phosphate is converted to fructose 6-phosphate by triosephosphate isomerase and phosphoglucose isomerase.

Ligases:

These enzymes carry out a task that is the exact opposite of what hydrolases do. Ligases create bonds by removing the water component, whereas hydrolases break bonds by adding water. There are various ligase subclasses that are involved in ATP synthesis

Working of an Enzyme

Energy is necessary for all reactions in the universe to take place. When there is no activation energy present, a catalyst is crucial in lowering the activation energy and advancing the reaction. Both plants and animals can benefit from this. Enzymes aid in lowering the reaction's complicated molecules' activation energy.

Step 1: One of the substrate molecules can bind to an "active site" that each enzyme has. An enzyme-substrate complex is created as a result.

Step 2: This reaction between the enzyme-substrate molecule and the second substrate results in the formation of the product, and the enzyme is released as the second product. The enzyme remains unaltered and is released as it is after the completion of the reaction.

There are certain theories that support the working of an enzyme. Primarily two theories are well accepted.

Theory 1: Lock and Key theory

According to this view, an enzyme-substrate complex is formed when the substrate precisely fits into the enzyme's active site. This approach also explains why enzymes are so specialised in the substances they target as their substrates because are specific to particular substrates similar to how each lock has a specific key for its working and no one key can open or close every lock.

Theory 2: Induced Fit Theory

The lock and key theory and this are comparable. According to this theory, the shape of the enzyme molecule alters as it approaches the substrate molecule, allowing the substrate to perfectly fit into the enzyme's active site.

Factors Affecting Enzymes

1. The concentration of Substrates and Enzymes:

Up until a certain point, the rate of reaction increases with rising substrate concentration; after that point, any additional increase in substrate concentration has little to no effect on the rate of reaction. This happens because there is a point at which the enzyme's active sites are entirely occupied and no more reactions can take place.

2. Temperature:

The molecules' increased kinetic energy causes the enzyme activity to rise as the temperature rises. The best and most efficient degree of enzyme activity exists. This temperature is frequently the body's natural temperature. Enzymes, which are composed of proteins, start to break down when the temperature rises above a particular point, slowing the rate of response.

3. pH:

Enzymes have a very narrow range of acceptable pH values and are extremely sensitive to pH fluctuations. The risk of the enzymes dissolving below or above the ideal pH level causes the reaction to slow down.

4. Inhibitors:

Substances that prevent a specific enzyme from performing its function. This happens when the chemical that inhibits the enzyme connects to its active site, preventing the substrate from attaching and slowing down the reaction.

Conclusion

Enzymes are therefore vital for body metabolic activities since they are eager participants in the digestion process, respiration, DNA replication, cell regulation, and many more. They carry out 6 major functions and there is one more type that is less known called translocases which catalyze ion movements across membranes.